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Ligand putidaredoxin

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (2 results)

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Show Natural Substrate (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.15.1

(+)-camphor + putidaredoxin + O2 = (R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O

347690, 347691, 347692, 347693, 347694, 347695, 347697, 347701, 347702, 347704, 347705, 347706, 347707, 347708, 347710, 347713

-

1.14.15.1

(1R)-camphor + putidaredoxin + O2 = 5-exo-(1R)-hydroxycamphor + oxidized putidaredoxin + H2O

713450

-

1.14.15.1

2 entries

Substrate in Enzyme-catalyzed Reactions (37 results)

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Show Substrate (37 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.15.1

(+)-alpha-pinene + putidaredoxin + O2 = (+)-cis-verbenol + (+)-myrtenol + (+)-verbenone + oxidized putidaredoxin + H2O

658971

-

1.14.15.1

(+)-alpha-pinene + putidaredoxin + O2 = ? + oxidized putidaredoxin + H2O

657898

-

1.14.15.1

(+)-camphor + putidaredoxin + O2 = (R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O

658056, 347690, 347691, 347692, 347693, 347694, 347695, 347697, 347701, 347702, 347704, 347705, 347706, 347707, 347708, 347710, 347713

-

1.14.15.1

(1R)-5,5-difluorocamphor + putidaredoxin + O2 = ? + oxidized putidaredoxin + H2O

657684

-

1.14.15.1

(1R)-5-exo-methoxycamphor + putidaredoxin + O2 = ? + oxidized putidaredoxin + H2O

657684

-

1.14.15.1

(1R)-5-methylenylcamphor + putidaredoxin + O2 = ? + oxidized putidaredoxin + H2O

657684

-

1.14.15.1

(1R)-camphor + putidaredoxin + O2 = 5-exo-(1R)-hydroxycamphor + oxidized putidaredoxin + H2O

713450

-

1.14.15.1

(1R)-camphor + putidaredoxin + O2 = ? + oxidized putidaredoxin + H2O

659635, 657684

-

1.14.15.1

(1R)-camphor enol ether + putidaredoxin + O2 = ? + oxidized putidaredoxin + H2O

659635

-

1.14.15.1

(1R)-camphor N-methyl imine + putidaredoxin + O2 = ? + oxidized putidaredoxin + H2O

659635

-

1.14.15.1

(1R)-camphor oxime + putidaredoxin + O2 = ? + oxidized putidaredoxin + H2O

659635

-

1.14.15.1

(1R)-endo-borneol allyl ether + putidaredoxin + O2 = ? + oxidized putidaredoxin + H2O

659635

-

1.14.15.1

(1R)-endo-borneol methyl ether + putidaredoxin + O2 = ? + oxidized putidaredoxin + H2O

659635

-

1.14.15.1

(1R)-endo-borneol propyl ether + putidaredoxin + O2 = ? + oxidized putidaredoxin + H2O

659635

-

1.14.15.1

(1R)-iso-borneol methyl ether + putidaredoxin + O2 = ? + oxidized putidaredoxin + H2O

659635

-

1.14.15.1

(1R)-norcamphor + putidaredoxin + O2 = ? + oxidized putidaredoxin + H2O

657684

-

1.14.15.1

(1S)-camphor + putidaredoxin + O2 = ? + oxidized putidaredoxin + H2O

657684

-

1.14.15.1

(4S)-limonene + putidaredoxin + O2 = ?

702820

-

1.14.15.1

(R)-3-ethylhexanol + putidaredoxin + O2 = 2-ethylhexanoic acid + 2-ethyl-1,2-hexanediol + 2-ethyl-1,3-hexanediol + 2-ethyl-1,4-hexanediol + oxidized putidaredoxin + H2O

347707

-

1.14.15.1

(S)-3-ethylhexanol + putidaredoxin + O2 = 2-ethylhexanoic aicd + 2-ethyl-1,2-hexanediol + 2-ethyl-1,3-hexanediol + 2-ethyl-1,4-hexanediol + oxidized putidaredoxin + H2O

347707

-

1.14.15.1

1,2,4,5-tetrachlorobenzene + putidaredoxin + O2 = 2,3,5,6-tetrachlorophenol + oxidized putidaredoxin + H2O

347708

-

1.14.15.1

1,2-campholide + putidaredoxin + O2 = 5-exo-hydroxy-1,2-campholide + oxidized putidaredoxin + H2O

347690, 347691

-

1.14.15.1

1,2-dichlorobenzene + putidaredoxin + O2 = 2,3-dichlorophenol + 3,4-dichlorophenol + oxidized putidaredoxin + H2O

347708

-

1.14.15.1

1,3,5-trichlorobenzene + putidaredoxin + O2 = 2,4,6-trichlorophenol + oxidized putidaredoxin + H2O

347708

-

1.14.15.1

1,3,5-trichlorobenzene + putidaredoxin + O2 = ? + oxidized putidaredoxin + H2O

657898

-

1.14.15.1

1,3-dichlorobenzene + putidaredoxin + O2 = 2,6-dichlorophenol + 2,4-dichlorophenol + 2,5-dichlorophenol + 2,3-dichlorophenol + oxidized putidaredoxin + H2O

347708

-

1.14.15.1

1,4-dichlorobenzene + putidaredoxin + O2 = 2,5-dichlorophenol + oxidized putidaredoxin + H2O

347708

-

1.14.15.1

1-dehydrocamphor + putidaredoxin + O2 = exo-5,6-epoxycamphor + oxidized putidaredoxin + H2O

347694

-

1.14.15.1

5,5-difluorocamphor + putidaredoxin + O2 = 5,5-difluoro-9-hydroxycamphor + oxidized putidaredoxin + H2O

347695

-

1.14.15.1

5-exo-bromocamphor + putidaredoxin + O2 = 5-ketocamphor + oxidized putidaredoxin + Br- + H2O

347693

-

1.14.15.1

adamantanone + putidaredoxin + O2 = ? + oxidized putidaredoxin + H2O

657684

-

1.14.15.1

benzo[a]pyrene + putidaredoxin + O2 = 3-hydroxybenzo[a]pyrene + oxidized putidaredoxin + H2O

347709

-

1.14.15.1

ethylbenzene + putidaredoxin + O2 = 1-phenylethanol + oxidized putidaredoxin + H2O

347702

-

1.14.15.1

fluoranthene + putidaredoxin + O2 = 3-fluoranthol + oxidized putidaredoxin + H2O

347709

-

1.14.15.1

phenanthrene + putidaredoxin + O2 = 1-phenanthrol + 2-phenanthrol + 3-phenanthrol + 4-phenanthrol + oxidized putidaredoxin + H2O

347709

-

1.14.15.1

pyrene + putidaredoxin + O2 = 1-pyrenol + 2-pyrenol + 1,6-pyrenequinone + 1,8-pyrenequinone + oxidized putidaredoxin + H2O

347709

-

1.14.15.1

36 entries

1.18.1.5

putidaredoxin + NADH = ?

681373

-

Product in Enzyme-catalyzed Reactions (1 result)

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Show Product (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.15.1

1,2-dibromo-3-chloropropane + O2 + reduced putidaredoxin = 1-bromo-3-chloroacetone + allyl chloride + H2O + putidaredoxin + Br-

0

-

Enzyme Cofactor/Cosubstrate (19 results)

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Show Cofactor (19 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.15.1

-

347695, 347697, 347698, 347699, 347700, 671535, 672760, 673037, 673071, 674152, 674438, 674474, 674959, 675234, 676280, 702301, 702820, 704713, 705331, 724338, 725602, 725873, 701873, 671612, 672083, 673054, 674197, 675233, 676941, 701533, 701902, 702698, 704181, 744343, 744365, 744704, 745613, 746282

-

1.14.15.1

analysis of protein-protein interactions between enzyme and cofactor, structural changes upon complex formation, overview

672413

-

1.14.15.1

binding causes conformational changes involving K+, in absence of K+ multiple conformations occur, overview

672100

-

1.14.15.1

binding of putidaredoxin converts a single X-proline amide bond in CYP101 from trans or distorted trans to cis

706783

-

1.14.15.1

cannot be replaced by other FeS-proteins or the phospholipid of the hepatic microsomal P450 system

347691

-

1.14.15.1

cofactor putidaredxin-bound enzyme structure analysis using crystal structure, PDB ID 4JWS

746306

-

1.14.15.1

electron transfer from putidaredoxin to the ferric-superoxo enzyme form, overview

672115

-

1.14.15.1

essential, iron-sulfur redox protein, Fe2S2*Cys4-class, e-transfer agent to and effector of cytochrome P450cam

347692, 347693

-

1.14.15.1

optimal ratio of putidaredoxin reductase, putidaredoxin, cytochrome m is 1:10:2

702799

-

1.14.15.1

Pdx, the enzyme is highly specific for its reductase, with an absolute requirement for the native putidaredoxin (Pdx) to provide the second electron transfer, binding kinetics and thermodynamics with wild-type and mutant enzymes, overview. Upon binding ferric P450cam, Pdx is now known to trigger a conformational change in the enzyme, which may provide the trigger to coordinate enzyme turnover and protect the enzyme from oxidative damage

744192

-

1.14.15.1

the catalytic cycle of P450cam requires two electrons, both of which are donated by putidaredoxin (Pdx), a ferredoxin containing a [2Fe-2S] cluster, structures of the Pdx-P450cam complex, potential electron transfer pathways and interactions between Pdx Asp38 and P450cam Arg112, as well as hydrophobic contacts between the Pdx Trp106 and P450cam residues, favorable interactions exist between Pdx Tyr33 and P450cam Asp125, as well as between Pdx Ser42 and P450cam His352, overview

744698

-

1.14.15.1

the physiological electron transfer partner protein contains a [2Fe-2S] cluster, energetic importance and role of the polar residues, e.g. Tyr33, involved in the Pdx-P450cam interaction, overview. Interaction key residues are Pdx Asp38, Arg66, and Trp106, as well as P450cam Arg109 and Arg112, crystal structure of the Pdx-P450cam complex

724762

-

1.14.15.1

the physiological reductant and effector

672144

-

1.14.15.1

the putidaredoxin-binding site is only minimally affected by cytochrome b5

347705

-

1.14.15.1

the reaction cycle requires two distinct electron transfer processes from the [2Fe-2S] containing putidaredoxin to P450cam, altered binding and electron transfer with the putidaredoxin mutant C73S, structure and model of oxidized and reduced forms, overview

672070

-

1.14.15.1

the substrate-free oxyferrous enzyme also reacts readily with reduced putidaredoxin

674516

-

1.14.15.1

transferring electrons from NADH to P450cam in a coupled assay method

713450

-

1.14.15.1

wild-type and mutant C73S/C85S cofactor, the mutant shows about 2fold improved substrate conversion

672742

-

1.14.15.1

[2Fe-2S] putidaredoxin, Pdx. Camphor-bound ferric P450cam domain forms a complex with Pdx, modeling

744637

-

1.14.15.1

19 entries

Inhibitor in Enzyme-catalyzed Reactions (1 result)

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Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.15.1

-

658056

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (1 result)

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Show Turnover Number (1 entry)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.14.15.1

2

-

constituent protein of the multi-component oxygenase

347692

K_i Value (2 results)

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Show KI Value (2 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.14.15.1

0.00038

-

recombinant enzyme with His6-tag, pH 7.4, 25°C

658056

1.14.15.1

0.0007

-

wild-type, pH 7.4, 25°C

658056

1.14.15.1

2 entries

References & Links

Literature References (74)

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Show Reference (74 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

347690

4378858

Mixed function oxidation. IV. An induced methylene hydroxylase in camphor oxidation

1965

Hedegaard, J.; Gunsalus, I.C.

J. Biol. Chem.

240

4038-4043

347691

4341491

The role of putidaredoxin and P450 cam in methylene hydroxylation

1972

Tyson, C.T.; Lipscomb, J.D.; Gunsalus, I.C.

J. Biol. Chem.

247

5777-5784

347692

672627

Bacterial P-450cam methylene monooxygenase components: cytochrome m, putidaredoxin, and putidaredoxin reductase

1978

Gunsalus, I.C.; Wagner, G.C.

Methods Enzymol.

52

166-188

347693

7240237

Interaction of 5-bromocamphor with cytochrome P-450 cam. Production of 5-ketocamphor from a mixed spin state hemoprotein

1981

Gould, P.V.; Gelb, M.H.; Sligar, S.G.

J. Biol. Chem.

256

6686-6691

347694

7073732

Cytochrome P450cam catalyzed epoxidation of dehydrocamphor

1982

Gelb, M.H.; Mälkönen, P.; Sligar, S.G.

Biochem. Biophys. Res. Commun.

104

853-858

347695

6501299

Novel reactivity of cytochrome P-450-CAM. Methyl hydroxylation of 5,5-difluorocamphor

1984

Smith Eble, K.; Dawson, J.H.

J. Biol. Chem.

259

14389-14393

347697

7074020

Stereochemistry and deuterium isotope effects in camphor hydroxylation by the cytochrome P450cam monoxygenase system

1982

Gelb, M.H.; Heimbrook, D.C.; Mälkönen, P.; Sligar, S.G.

Biochemistry

21

370-377

347698

4332595

Composition and structure of camphor hydroxylase components and homology between putidaredoxin and adrenodoxin

1971

Tsai, R.L.; Gunsalus, I.C.; Dus, K.

Biochem. Biophys. Res. Commun.

45

1300-1306

347699

4385345

Reduction of palmitoyl dihydroxyacetone phosphate by mitochondria

1968

Katagiri, M.; Ganguli, B.N.; Gunsalus, I.C.

J. Biol. Chem.

243

3542-3555

347700

4335959

Pseudomonas putida cytochrome P-450: characterization of an oxygenated form of the hemoprotein

1972

Peterson, J.A.; Ishimura, Y.; Griffith, B.W.

Arch. Biochem. Biophys.

149

197-208

347701

11051559

Roles of the axial push effect in cytochrome P450cam studied with the site-directed mutagenesis at the heme proximal site

2000

Yoshioka, S.; Takahashi, S.; Ishimori, K.; Morishima, I.

J. Inorg. Biochem.

81

141-151

347702

8475046

Engineering cytochrome P-450cam to increase the stereospecificity and coupling of aliphatic hydroxylation

1993

Loida, P.J.; Sligar, S.G.

Protein Eng.

6

207-212

347704

10698731

The catalytic pathway of cytochrome P450cam at atomic resolution

2000

Schlichting, I.; Berendzen, J.; Chu, K.; Stock, A.M.; Maves, S.A.; Benson, D.E.; Sweet, R.M.; Ringe, D.; Petsko, G.A.; Sligar, S.G.

Science

287

1615-1622

347705

11706033

Complex formation of cytochrome P450cam with putidaredoxin: evidence for protein-specific interactions involving the proximal thiolate ligand

2002

Unno, M.; Christian, J.F.; Sjodin, T.; Benson, D.E.; Macdonald, I.D.G.; Sligar, S.G.; Champion, P.M.

J. Biol. Chem.

277

2547-2553

347706

9542996

The dimerization of Pseudomonas putida cytochrome P450cam: practical consequences and engineering of a monomeric enzyme

1997

Nickerson, D.P.; Wong, L.L.

Protein Eng.

10

1357-1361

347707

11583152

Benign synthesis of 2-ethylhexanoic acid by cytochrome P450cam: enzymatic, crystallographic, and theoretical studies

2001

French, K.J.; Strickler, M.D.; Rock, D.A.; Rock, D.A.; Bennett, G.A.; Wahlstrom, J.L.; Goldstein, B.M.; Jones, J.P.

Biochemistry

40

9532-9538

347708

11231299

Oxidation of polychlorinated benzenes by genetically engineered CYP101 (cytochrome P450(cam))

2001

Jones, J.P.; O'Hare, E.J.; Wong, L.L.

Eur. J. Biochem.

268

1460-1467

347709

10708651

Protein engineering of cytochrome p450(cam) (CYP101) for the oxidation of polycyclic aromatic hydrocarbons

2000

Harford-Cross, C.F.; Carmichael, A.B.; Allan, F.K.; England, P.A.; Rouch, D.A.; Wong, L.L.

Protein Eng.

13

121-128

347710

11168358

Proximal cysteine residue is essential for the enzymatic activities of cytochrome P450cam

2001

Yoshioka, S.; Takahashi, S.; Hori, H.; Ishimori, K.; Morishima, I.

Eur. J. Biochem.

268

252-259

347713

10371217

Surface-modified mutants of cytochrome p450cam enzymatic properties and electrochemistry

1999

Lo, K.K.; Wong, L.L.; Hill, A.O.

FEBS Lett.

451

342-346

657684

15752707

The influence of substrate on the spectral properties of oxyferrous wild-type and T252A cytochrome P450-CAM

2005

Sono, M.; Perera, R.; Jin, S.; Makris, T.M.; Sligar, S.G.; Bryson, T.A.; Dawson, J.H.

Arch. Biochem. Biophys.

436

40-49

657898

12773156

Engineering substrate recognition in catalysis by cytochrome P450cam

2003

Bell, S.G.; Chen, X.; Xu, F.; Rao, Z.; Wong, L.L.

Biochem. Soc. Trans.

31

558-562

658056

14705955

Steady-state kinetic investigation of cytochrome P450cam: interaction with redox partners and reaction with molecular oxygen

2004

Purdy, M.M.; Koo, L.S.; Ortiz de Montellano, P.R.; Klinman, J.P.

Biochemistry

43

271-281

658971

12526670

Molecular recognition in (+)-alpha-pinene oxidation by cytochrome P450cam

2003

Bell, S.G.; Chen, X.; Sowden, R.J.; Xu, F.; Williams, J.N.; Wong, L.L.; Rao, Z.

J. Am. Chem. Soc.

125

705-714

659635

12237225

Specific and non-specific effects of potassium cations on substrate-protein interactions in cytochromes P450cam and P450lin

2002

Deprez, E.; Gill, E.; Helms, V.; Wade, R.C.; Hui Bon Hoa, G.

J. Inorg. Biochem.

91

597-606

671535

16421717

A recombinant Escherichia coli whole cell biocatalyst harboring a cytochrome P450cam monooxygenase system coupled with enzymatic cofactor regeneration

2006

Mouri, T.; Michizoe, J.; Ichinose, H.; Kamiya, N.; Goto, M.

Appl. Microbiol. Biotechnol.

72

514-520

671612

17049478

Effect of alcohols on binding of camphor to cytochrome P450cam: spectroscopic and stopped flow transient kinetic studies

2006

Murugan, R.; Mazumdar, S.

Arch. Biochem. Biophys.

455

154-162

672070

17002293

Putidaredoxin-to-cytochrome P450cam electron transfer: differences between the two reductive steps required for catalysis

2006

Kuznetsov, V.Y.; Poulos, T.L.; Sevrioukova, I.F.

Biochemistry

45

11934-11944

672083

17042489

Role of threonine 101 on the stability of the heme active site of cytochrome P450cam: multiwavelength circular dichroism studies

2006

Manna, S.K.; Mazumdar, S.

Biochemistry

45

12715-12722

672100

17128977

Specific effects of potassium ion binding on wild-type and L358P cytochrome P450cam

2006

OuYang, B.; Pochapsky, S.S.; Pagani, G.M.; Pochapsky, T.C.

Biochemistry

45

14379-14388

672115

17176102

Mechanism of O2 activation by cytochrome P450cam studied by isotope effects and transient state kinetics

2006

Purdy, M.M.; Koo, L.S.; Montellano, P.R.; Klinman, J.P.

Biochemistry

45

15793-15806

672144

16548516

Comparison of the complexes formed by cytochrome P450cam with cytochrome b5 and putidaredoxin, two effectors of camphor hydroxylase activity

2006

Rui, L.; Pochapsky, S.S.; Pochapsky, T.C.

Biochemistry

45

3887-3897

672413

17014964

FTIR studies of the redox partner interaction in cytochrome P450: the Pdx-P 450cam couple

2007

Karyakin, A.; Motiejunas, D.; Wade, R.C.; Jung, C.

Biochim. Biophys. Acta

1770

420-431

672742

16955357

Increasing the catalytic performance of a whole cell biocatalyst harboring a cytochrome p450cam system by stabilization of an electron transfer component

2006

Mouri, T.; Kamiya, N.; Goto, M.

Biotechnol. Lett.

28

1509-1513

672760

16080691

Effect of oxygen on the dehalogenation of 1,2-dibromo-3-chloropropane by cytochrome P450cam (CYP101)

2005

Koe, G.S.; Vilker, V.L.

Biotechnol. Prog.

21

1119-1127

673037

16027900

Identification of broad specificity P450CAM variants by primary screening against indole as substrate

2005

Celik, A.; Speight, R.E.; Turner, N.J.

Chem. Commun. (Camb. )

2005

3652-3654

673054

-

Substrate binding in the active site of cytochrome P450cam

2005

Swart, M.; Groenhof, A.R.; Ehlers, A.W.; Lammertsma, K.

Chem. Phys. Lett.

403

35-41

673071

15912551

Structure and redox properties of the haem centre in the C357M mutant of cytochrome P450cam

2005

Murugan, R.; Mazumdar, S.

ChemBioChem

6

1204-1211

674152

15686372

Substrate modulation of the properties and reactivity of the oxy-ferrous and hydroperoxo-ferric intermediates of cytochrome P450cam as shown by cryoreduction-EPR/ENDOR spectroscopy

2005

Davydov, R.; Perera, R.; Jin, S.; Yang, T.C.; Bryson, T.A.; Sono, M.; Dawson, J.H.; Hoffman, B.M.

J. Am. Chem. Soc.

127

1403-1413

674197

16551096

The effect of heme environment on the hydrogen abstraction reaction of camphor in P450cam catalysis: a QM/MM study

2006

Altun, A.; Guallar, V.; Friesner, R.A.; Shaik, S.; Thiel, W.

J. Am. Chem. Soc.

128

3924-3925

674438

15781454

Reaction of ferric cytochrome P450cam with peracids: kinetic characterization of intermediates on the reaction pathway

2005

Spolitak, T.; Dawson, J.H.; Ballou, D.P.

J. Biol. Chem.

280

20300-20309

674474

15994329

Crystallographic study on the dioxygen complex of wild-type and mutant cytochrome P450cam. Implications for the dioxygen activation mechanism

2005

Nagano, S.; Poulos, T.L.

J. Biol. Chem.

280

31659-31663

674516

16115886

Direct observation of a novel perturbed oxyferrous catalytic intermediate during reduced putidaredoxin-initiated turnover of cytochrome P-450-CAM: probing the effector role of putidaredoxin in catalysis

2005

Glascock, M.C.; Ballou, D.P.; Dawson, J.H.

J. Biol. Chem.

280

42134-42141

674959

16233747

Functionalization of the cytochrome P450cam monooxygenase system in the cell-like aqueous compartments of water-in-oil emulsions

2005

Michizoe, J.; Ichinose, H.; Kamiya, N.; Maruyama, T.; Goto, M.

J. Biosci. Bioeng.

99

12-17

675233

17095096

Rapid kinetics investigations of peracid oxidation of ferric cytochrome P450cam: nature and possible function of compound ES

2006

Spolitak, T.; Dawson, J.H.; Ballou, D.P.

J. Inorg. Biochem.

100

2034-2044

675234

17084458

On the identity and reactivity patterns of the "second oxidant" of the T252A mutant of cytochrome P450cam in the oxidation of 5-methylenenylcamphor

2006

Hirao, H.; Kumar, D.; Shaik, S.

J. Inorg. Biochem.

100

2054-2068

676280

17047872

Mechanisms of reaction in cytochrome P450: hydroxylation of camphor in P450cam

2006

Zurek, J.; Foloppe, N.; Harvey, J.N.; Mulholland, A.J.

Org. Biomol. Chem.

4

3931-3937

676941

16943206

Cytochrome P450 active site plasticity: attenuation of imidazole binding in cytochrome P450(cam) by an L244A mutation

2006

Verras, A.; Alian, A.; de Montellano, P.R.

Protein Eng. Des. Sel.

19

491-496

681373

15095867

Crystal structure of putidaredoxin reductase from Pseudomonas putida, the final structural component of the cytochrome P450cam monooxygenase

2004

Sevrioukova, I.F.; Li, H.; Poulos, T.L.

J. Mol. Biol.

336

889-902

701533

19193991

Substrate binding induces structural changes in cytochrome P450cam

2009

Sakurai, K.; Shimada, H.; Hayashi, T.; Tsukihara, T.

Acta Crystallogr. Sect. F

65

80-83

701873

19779713

A cytochrome P450 class I electron transfer system from Novosphingobium aromaticivorans

2010

Bell, S.G.; Dale, A.; Rees, N.H.; Wong, L.L.

Appl. Microbiol. Biotechnol.

86

163-175

701902

18359283

Efficient catalytic turnover of cytochrome P450(cam) is supported by a T252N mutation

2008

Kim, D.; Heo, Y.S.; Ortiz de Montellano, P.R.

Arch. Biochem. Biophys.

474

150-156

702301

19366254

Redox-dependent dynamics in cytochrome P450cam

2009

Pochapsky, S.S.; Dang, M.; OuYang, B.; Simorellis, A.K.; Pochapsky, T.C.

Biochemistry

48

4254-4261

702698

18395959

Roles of two surface residues near the access channel in the substrate recognition by cytochrome P450cam

2008

Behera, R.K.; Mazumdar, S.

Biophys. Chem.

135

1-6

702799

18098319

P450cam biocatalysis in surfactant-stabilized two-phase emulsions

2008

Ryan, J.; Clark, D.

Biotechnol. Bioeng.

99

1311-1319

702820

19458919

Tricistronic overexpression of cytochrome P450cam, putidaredoxin, and putidaredoxin reductase provides a useful cell-based catalytic system

2009

Kim, D.; Ortiz de Montellano, P.R.

Biotechnol. Lett.

31

1427-1431

704181

19133773

A role of the heme-7-propionate side chain in cytochrome P450cam as a gate for regulating the access of water molecules to the substrate-binding site

2009

Hayashi, T.; Harada, K.; Sakurai, K.; Shimada, H.; Hirota, S.

J. Am. Chem. Soc.

131

1398-1400

704713

18273651

Replacement of tyrosine residues by phenylalanine in cytochrome P450cam alters the formation of Cpd II-like species in reactions with artificial oxidants

2008

Spolitak, T.; Dawson, J.H.; Ballou, D.P.

J. Biol. Inorg. Chem.

13

599-611

705331

18543897

Multireference ab initio quantum mechanics/molecular mechanics study on intermediates in the catalytic cycle of cytochrome P450(cam)

2008

Altun, A.; Kumar, D.; Neese, F.; Thiel, W.

J. Phys. Chem. A

112

12904-12910

706783

18513977

A functional proline switch in cytochrome P450cam

2008

OuYang, B.; Pochapsky, S.S.; Dang, M.; Pochapsky, T.C.

Structure

16

916-923

713450

21273340

Changing the substrate specificity of P450cam towards diphenylmethane by semi-rational enzyme engineering

2011

Hoffmann, G.; Boensch, K.; Greiner-Stoeffele, T.; Ballschmiter, M.

Protein Eng. Des. Sel.

24

439-446

724338

22468842

Solution structural ensembles of substrate-free cytochrome P450(cam)

2012

Asciutto, E.K.; Young, M.J.; Madura, J.; Pochapsky, S.S.; Pochapsky, T.C.

Biochemistry

51

3383-3393

724762

24302683

Hot-spot residues in the cytochrome p450cam-putidaredoxin binding interface

2014

Hiruma, Y.; Gupta, A.; Kloosterman, A.; Olijve, C.; Olmez, B.; Hass, M.A.; Ubbink, M.

ChemBioChem

15

80-86

725602

21562741

Identification of camphor oxidation and reduction products in Pseudomonas putida: new activity of the cytochrome P450cam system

2011

Prasad, B.; Rojubally, A.; Plettner, E.

J. Chem. Ecol.

37

657-667

725873

21186391

Spring-loading the active site of cytochrome P450 cam

2011

Dang, M.; Pochapsky, S.; Pochapsky, T.

Metallomics

3

339-343

744192

26664590

Active site diversification of P450cam with indole generates catalysts for benzylic oxidation reactions

2015

Kelly, P.; Eichler, A.; Herter, S.; Kranz, D.; Turner, N.; Flitsch, S.

Beilstein J. Org. Chem.

11

1713-1720

744343

26460790

Kinetic consequences of introducing a proximal selenocysteine ligand into cytochrome P450cam

2015

Vandemeulebroucke, A.; Aldag, C.; Stiebritz, M.; Reiher, M.; Hilvert, D.

Biochemistry

54

6692-6703

744365

28581729

Conformational heterogeneity and the affinity of substrate molecular recognition by cytochrome P450cam

2017

Basom, E.; Manifold, B.; Thielges, M.

Biochemistry

56

3248-3256

744637

28944003

Partial fusion of a cytochrome P450 system by carboxy-terminal attachment of putidaredoxin reductase to P450cam (CYP101A1)

2016

Johnson, E.O.; Wong, L.L.

Catal. Sci. Technol.

6

7549-7560

744698

24302683

Hot-spot residues in the cytochrome P450cam-putidaredoxin binding interface

2014

Hiruma, Y.; Gupta, A.; Kloosterman, A.; Olijve, C.; Oelmez, B.; Hass, M.; Ubbink, M.

ChemBioChem

15

80-86

744704

26698167

Enantioselective benzylic hydroxylation catalysed by P450 monooxygenases characterisation of a P450cam mutant library and molecular modelling

2016

Eichler, A.; Gricman, Å.; Herter, S.; Kelly, P.; Turner, N.; Pleiss, J.; Flitsch, S.

ChemBioChem

17

426-432

745613

25955684

Conformational landscape and the selectivity of cytochrome P450cam

2015

Basom, E.; Spearman, J.; Thielges, M.

J. Phys. Chem. B

119

6620-6627

746282

19293375

Probing the role of the proximal heme ligand in cytochrome P450cam by recombinant incorporation of selenocysteine

2009

Aldag, C.; Gromov, I.A.; Garcia-Rubio, I.; von Koenig, K.; Schlichting, I.; Jaun, B.; Hilvert, D.

Proc. Natl. Acad. Sci. USA

106

5481-5486

746306

26130807

Delicate conformational balance of the redox enzyme cytochrome P450cam

2015

Skinner, S.; Liu, W.; Hiruma, Y.; Timmer, M.; Blok, A.; Hass, M.; Ubbink, M.

Proc. Natl. Acad. Sci. USA

112

9022-9027

Links to other databases for putidaredoxin

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