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show all sequences of 1.8.99.5

The octahaem MccA is a haem c-copper sulfite reductase

Hermann, B.; Kern, M.; La Pietra, L.; Simon, J.; Einsle, O.; Nature 520, 706-709 (2015)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
purified enzyme, X-ray diffraction structure determination and analysis at 2.2 A resolution, single-wavelength anomalous dispersion
Wolinella succinogenes
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Cu
the heterobimetallic active-site heme 2 has a Cu(I) ion juxtaposed to a heme c at a Fe-Cu distance of 4.4 A. While the combination of metals is reminiscent of respiratory heme–copper oxidases, the oxidation-labile Cu(I) centre of MccA does not seem to undergo a redox transition during catalysis. The copper-depleted form II of MccA, the absence of the heterometal allows for a binding mode of sulfite that is similar to the one seen in the siroheme-containing enzymes or in NrfA. In the structure of the Cu-containing, high-activity form I of MccA, all 12 monomers in the asymmetric unit have a ligand bound to heme 2
Wolinella succinogenes
Fe
the heterobimetallic active-site heme 2 has a Cu(I) ion juxtaposed to a heme c at a Fe-Cu distance of 4.4 A
Wolinella succinogenes
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Wolinella succinogenes
multiheme cytochrome c enzymes catalyse complex-multi-electron redox reactions and bind their substrates through the free electron pairs of a heteroatom to a free coordination position at an active-site hem group. Electrons are then provided or accepted by the tightly coupled chain of heme groups
?
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sulfite + 6 ferrocytochrome c + 6 H+
Wolinella succinogenes
overall transfer of 6 electrons during the reaction
sulfide + 6 ferricytochrome c + 3 H2O
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?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Wolinella succinogenes
Q7MSJ8
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Reaction
Reaction
Commentary
Organism
hydrogen sulfide + a [DsrC protein]-disulfide + 2 acceptor + 3 H2O = sulfite + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+
sulfite is bound at an oxidation state of S1IV and immediately dehydrated. All oxygen atoms are fixed in a tight hydrogen-bonding network, upon transfer of two electrons to yield an S1II state, a second oxygen atom is released as water, but held within the active-site cavity. A further two-electron reduction leads to the S0 state, weakening the remaining S-O bond. With the final transfer of two electrons, the state of sulfide (S2II) is reached and a third water is released, catalytic mechanism overview. The heterobimetallic active-site heme 2 has a Cu(I) ion juxtaposed to a heme c at a Fe-Cu distance of 4.4 A. While the combination of metals is reminiscent of respiratory heme-copper oxidases, the oxidation-labile Cu(I) centre of MccA does not seem to undergo a redox transition during catalysis. Intact MccA tightly binds SO2 at heme 2, a dehydration product of the substrate sulfite that is partially turned over due to photoreduction by X-ray irradiation, yielding the reaction intermediate SO. Structure of sulfite reduction at heme2 of MccA, sulfite binds to the resting state of the enzyme, but the active-site architecture shifts the reversible dehydration equilibrium to SO2 + H2O. Reduction by two electrons occurs through photoreduction in the X-ray beam and leads to release of a second H2O after protonation, with SO remaining bound to the active site. A tight network of hydrogen bonds surrounds the bimetal centre and the bound substrate, holding the reaction products in place. The sulfite substrate only oxidizes half the heme groups of reduced MccA, emphasizing that the total electron charge of the multiheme enzyme is of high relevance for catalysis
Wolinella succinogenes
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
multiheme cytochrome c enzymes catalyse complex-multi-electron redox reactions and bind their substrates through the free electron pairs of a heteroatom to a free coordination position at an active-site hem group. Electrons are then provided or accepted by the tightly coupled chain of heme groups
743347
Wolinella succinogenes
?
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additional information
MccA reduces sulfite, but not arsenate, selenate, selenite, hydroxylamine, hydrazine, fumarate, nitrate, thiosulfate, tetrathionate, polysulfide, or Fe(III). Nitrite is reduced only very slowly to ammonium
743347
Wolinella succinogenes
?
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-
sulfite + 6 ferrocytochrome c + 6 H+
overall transfer of 6 electrons during the reaction
743347
Wolinella succinogenes
sulfide + 6 ferricytochrome c + 3 H2O
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?
Subunits
Subunits
Commentary
Organism
homotrimer
with an unprecedented fold and heme arrangement, three-dimensional structure analysis
Wolinella succinogenes
More
in the CX15CH motif of heme 8, the extended region between the two cysteine residues forms a loop with a short helical turn, in direct vicinity to another loop harbouring the only non-proline cis peptide in the enzyme, between residues G508 and F509. Its formation might require the essential peptidyl isomerase MccB2, and it is presumed to be a prerequisite for correct folding of the loop in the maturation process of heme 8, which is likely to be attached by the dedicated cytochrome c synthase CcsA1. The structure of the CX15CH heme c binding motif disrupts the general parallel/perpendicular heme stacking sequence, and rotates the heme out of plane, possibly to optimize the interaction with the putative electron donor, the iron-sulfur protein MccC
Wolinella succinogenes
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome c
octaheme cytochrome
Wolinella succinogenes
heme
octaheme cytochrome, a homotrimer with an unprecedented fold and heme arrangement, as well as a heme bound to a CX15CH motif. The heterobimetallic active-site heme 2 has a Cu(I) ion juxtaposed to a heme c at a Fe-Cu distance of 4.4 A, active-site heme 2 is bound to a canonical CXXCH motif with H306 as a proximal axial ligand. In the CX15CH motif of heme 8, the extended region between the two cysteine residues forms a loop with a short helical turn, in direct vicinity to another loop harbouring the only non-proline cis peptide in the enzyme, between residues G508 and F509. Its formation might require the essential peptidyl isomerase MccB2, and it is presumed to be a prerequisite for correct folding of the loop in the maturation process of heme 8, which is likely to be attached by the dedicated cytochrome c synthase CcsA1. The structure of the CX15CH heme c binding motif disrupts the general parallel/perpendicular heme stacking sequence, and rotates the heme out of plane, possibly to optimize the interaction with the putative electron donor, the iron-sulfur protein MccC
Wolinella succinogenes
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome c
octaheme cytochrome
Wolinella succinogenes
heme
octaheme cytochrome, a homotrimer with an unprecedented fold and heme arrangement, as well as a heme bound to a CX15CH motif. The heterobimetallic active-site heme 2 has a Cu(I) ion juxtaposed to a heme c at a Fe-Cu distance of 4.4 A, active-site heme 2 is bound to a canonical CXXCH motif with H306 as a proximal axial ligand. In the CX15CH motif of heme 8, the extended region between the two cysteine residues forms a loop with a short helical turn, in direct vicinity to another loop harbouring the only non-proline cis peptide in the enzyme, between residues G508 and F509. Its formation might require the essential peptidyl isomerase MccB2, and it is presumed to be a prerequisite for correct folding of the loop in the maturation process of heme 8, which is likely to be attached by the dedicated cytochrome c synthase CcsA1. The structure of the CX15CH heme c binding motif disrupts the general parallel/perpendicular heme stacking sequence, and rotates the heme out of plane, possibly to optimize the interaction with the putative electron donor, the iron-sulfur protein MccC
Wolinella succinogenes
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified enzyme, X-ray diffraction structure determination and analysis at 2.2 A resolution, single-wavelength anomalous dispersion
Wolinella succinogenes
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Cu
the heterobimetallic active-site heme 2 has a Cu(I) ion juxtaposed to a heme c at a Fe-Cu distance of 4.4 A. While the combination of metals is reminiscent of respiratory heme–copper oxidases, the oxidation-labile Cu(I) centre of MccA does not seem to undergo a redox transition during catalysis. The copper-depleted form II of MccA, the absence of the heterometal allows for a binding mode of sulfite that is similar to the one seen in the siroheme-containing enzymes or in NrfA. In the structure of the Cu-containing, high-activity form I of MccA, all 12 monomers in the asymmetric unit have a ligand bound to heme 2
Wolinella succinogenes
Fe
the heterobimetallic active-site heme 2 has a Cu(I) ion juxtaposed to a heme c at a Fe-Cu distance of 4.4 A
Wolinella succinogenes
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Wolinella succinogenes
multiheme cytochrome c enzymes catalyse complex-multi-electron redox reactions and bind their substrates through the free electron pairs of a heteroatom to a free coordination position at an active-site hem group. Electrons are then provided or accepted by the tightly coupled chain of heme groups
?
-
-
-
sulfite + 6 ferrocytochrome c + 6 H+
Wolinella succinogenes
overall transfer of 6 electrons during the reaction
sulfide + 6 ferricytochrome c + 3 H2O
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
multiheme cytochrome c enzymes catalyse complex-multi-electron redox reactions and bind their substrates through the free electron pairs of a heteroatom to a free coordination position at an active-site hem group. Electrons are then provided or accepted by the tightly coupled chain of heme groups
743347
Wolinella succinogenes
?
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-
additional information
MccA reduces sulfite, but not arsenate, selenate, selenite, hydroxylamine, hydrazine, fumarate, nitrate, thiosulfate, tetrathionate, polysulfide, or Fe(III). Nitrite is reduced only very slowly to ammonium
743347
Wolinella succinogenes
?
-
-
-
-
sulfite + 6 ferrocytochrome c + 6 H+
overall transfer of 6 electrons during the reaction
743347
Wolinella succinogenes
sulfide + 6 ferricytochrome c + 3 H2O
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homotrimer
with an unprecedented fold and heme arrangement, three-dimensional structure analysis
Wolinella succinogenes
More
in the CX15CH motif of heme 8, the extended region between the two cysteine residues forms a loop with a short helical turn, in direct vicinity to another loop harbouring the only non-proline cis peptide in the enzyme, between residues G508 and F509. Its formation might require the essential peptidyl isomerase MccB2, and it is presumed to be a prerequisite for correct folding of the loop in the maturation process of heme 8, which is likely to be attached by the dedicated cytochrome c synthase CcsA1. The structure of the CX15CH heme c binding motif disrupts the general parallel/perpendicular heme stacking sequence, and rotates the heme out of plane, possibly to optimize the interaction with the putative electron donor, the iron-sulfur protein MccC
Wolinella succinogenes
General Information
General Information
Commentary
Organism
evolution
MccA belongs to the genetically diverse family of multiheme c enzymes and has eight heme groups covalently attached to conserved heme-binding motifs in the peptide sequence. Multiheme cytochrome c enzymes show a high conservation of heme group arrangements, but not of sequence, with recurring heme-packing motifs that result in either a parallel or a perpendicular packing of two of the moieties. They catalyse complexmulti-electron redox reactions and bind their substrates through the free electron pairs of a heteroatom to a free coordination position at an active-site hem group. Electrons are then provided or accepted by the tightly coupled chain of heme groups
Wolinella succinogenes
additional information
anoxically purified MccA exhibits a 2 to 5.5fold higher specific sulfite reductase activity than the enzyme isolated under oxic conditions. Presence of two cysteine residues, C399 and C495, juxtaposed at the distal side of the active-site cavity. The active site is a shallow cavity on the distal side of heme 2, lined by residues K208, Y285, Y301, R366 and K393, which are conserved among MccA orthologues
Wolinella succinogenes
physiological function
the Epsilonproteobacterium Wolinella succinogenes does not encode a siroheme sulfite reductase and the nrfA gene is not induced during sulfite respiration. Instead, sulfite is reduced by the octaheme c-type cytochrome MccA, with sulfide as the sole product. The enzyme MccA catalyzes the six-electron reduction of sulfite to sulfide, the pivot point of the biogeochemical cycle of the element sulfur for dissimilatory sulfite utilization. It is distinct from known sulfite reductases because it has a substantially higher catalytic activity and a relatively low reactivity towards nitrite
Wolinella succinogenes
General Information (protein specific)
General Information
Commentary
Organism
evolution
MccA belongs to the genetically diverse family of multiheme c enzymes and has eight heme groups covalently attached to conserved heme-binding motifs in the peptide sequence. Multiheme cytochrome c enzymes show a high conservation of heme group arrangements, but not of sequence, with recurring heme-packing motifs that result in either a parallel or a perpendicular packing of two of the moieties. They catalyse complexmulti-electron redox reactions and bind their substrates through the free electron pairs of a heteroatom to a free coordination position at an active-site hem group. Electrons are then provided or accepted by the tightly coupled chain of heme groups
Wolinella succinogenes
additional information
anoxically purified MccA exhibits a 2 to 5.5fold higher specific sulfite reductase activity than the enzyme isolated under oxic conditions. Presence of two cysteine residues, C399 and C495, juxtaposed at the distal side of the active-site cavity. The active site is a shallow cavity on the distal side of heme 2, lined by residues K208, Y285, Y301, R366 and K393, which are conserved among MccA orthologues
Wolinella succinogenes
physiological function
the Epsilonproteobacterium Wolinella succinogenes does not encode a siroheme sulfite reductase and the nrfA gene is not induced during sulfite respiration. Instead, sulfite is reduced by the octaheme c-type cytochrome MccA, with sulfide as the sole product. The enzyme MccA catalyzes the six-electron reduction of sulfite to sulfide, the pivot point of the biogeochemical cycle of the element sulfur for dissimilatory sulfite utilization. It is distinct from known sulfite reductases because it has a substantially higher catalytic activity and a relatively low reactivity towards nitrite
Wolinella succinogenes
Other publictions for EC 1.8.99.5
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
741984
Duarte
Electron transfer between the ...
Desulfovibrio desulfuricans
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1857
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Ghosh
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Intermolecular interaction stu ...
Allochromatium vinosum
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340
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742577
Leavitt
Sulfur isotope effects of dis ...
Archaeoglobus fulgidus, Desulfovibrio vulgaris, Desulfovibrio vulgaris DSM 644
Front. Microbiol.
6
1392
2015
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743347
Hermann
The octahaem MccA is a haem c ...
Wolinella succinogenes
Nature
520
706-709
2015
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743053
Lee
-
Construction of aligned datab ...
Chlorobium phaeobacteroides, Chlorobium phaeobacteroides BS1, Chlorobium phaeobacteroides DSM 266, Desulfitobacterium dichloroeliminans, Desulfitobacterium dichloroeliminans LMG P-21439, Desulfosporosinus orientis, Desulfosporosinus orientis DSM 765, Desulfovibrio vulgaris, Desulfovibrio vulgaris DP4, Desulfovibrio vulgaris Hildenborough, Thermaerobacter marianensis, Thermaerobacter marianensis AB011495
J. Korean Soc. Appl. Biol. Chem.
57
419-427
2014
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741792
Mori
Dominance of green sulfur bac ...
Candidatus Ruthia magnifica, Candidatus Thiobios zoothamnicoli, Chlorobium limicola, Chlorobium phaeovibrioides, Halochromatium salexigens, Magnetospirillum gryphiswaldense, Pelodictyon luteolum
Arch. Microbiol.
195
303-312
2013
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741814
Venceslau
Redox states of Desulfovibrio ...
Desulfovibrio vulgaris
Biochem. Biophys. Res. Commun.
441
732-736
2013
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725901
Holkenbrink
Sulfur globule oxidation in gr ...
Chlorobaculum tepidum, Chlorobaculum tepidum DSM 12025
Microbiology
157
1229-1239
2011
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1
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710741
Ogata
Purification, crystallization ...
Desulfovibrio vulgaris, Desulfovibrio vulgaris Miyazaki F
Acta Crystallogr. Sect. F
66
1470-1472
2010
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710943
Moreau
Diversity of dissimilatory sul ...
Soil bacterium
Appl. Environ. Microbiol.
76
4819-4828
2010
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1
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688412
Schiffer
Structure of the dissimilatory ...
Archaeoglobus fulgidus
J. Mol. Biol.
379
1063-1074
2008
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688700
Oliveira
Purification, crystallization ...
Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough
J. Struct. Biol.
164
236-239
2008
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698846
Oliveira
The crystal structure of Desul ...
Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough
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283
34141-34149
2008
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673621
Mander
X-ray structure of the gamma-s ...
Archaeoglobus fulgidus
FEBS Lett.
579
4600-4604
2005
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733771
Cort
Solution structure of Pyrobacu ...
Pyrobaculum aerophilum, Pyrobaculum aerophilum DSM 7523
Eur. J. Biochem.
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2001
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722213
Larsen
Dissimilatory sulfite reductas ...
Archaeoglobus profundus, Archaeoglobus profundus DSM 5631, Desulfofundulus thermocisternus
Extremophiles
3
63-70
1999
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734636
Pott
-
Sirohaem sulfite reductase and ...
Allochromatium vinosum, Allochromatium vinosum DSM 180
Microbiology
144
1881-1894
1998
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2
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1
1
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734637
Molitor
A dissimilatory sirohaem-sulfi ...
Pyrobaculum islandicum
Microbiology
144
529-541
1998
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4
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1
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733765
Marritt
Dissimilatory sulfite reductas ...
Desulfovibrio vulgaris
Eur. J. Biochem.
238
724-727
1996
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394066
Steuber
Molecular properties of the di ...
Desulfovibrio desulfuricans, Desulfovibrio desulfuricans Essex
Eur. J. Biochem.
233
873-879
1995
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2
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4
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5
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394063
Lui
Conformational gating of the d ...
Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough
Biochemistry
33
11209-11216
1994
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18
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2
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394068
Wolfe
Desulfoviridin, a multimeric-d ...
Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough
Eur. J. Biochem.
223
79-89
1994
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3
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20
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6
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6
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3
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3
3
394040
Seki
Characterization of a dissimil ...
Desulfovibrio africanus, Desulfovibrio africanus Benghazi
J. Biochem.
98
1535-1543
1985
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1
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394898
Harrison
Purification and characterizat ...
Clostridium pasteurianum
Arch. Microbiol.
138
72-78
1984
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4
1
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1
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1
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1
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394043
Hatchikian
Characterization of a new type ...
Thermodesulfobacterium commune
J. Bacteriol.
153
1211-1220
1983
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