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Information on EC 1.7.2.1 - nitrite reductase (NO-forming) and Organism(s) Pseudomonas aeruginosa and UniProt Accession P24474
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1.7.2.1 nitrite reductase (NO-forming)IUBMB Comments
The reaction is catalysed by two types of enzymes, found in the perimplasm of denitrifying bacteria. One type comprises proteins containing multiple copper centres, the other a heme protein, cytochrome cd1. Acceptors include c-type cytochromes such as cytochrome c-550 or cytochrome c-551 from Paracoccus denitrificans or Pseudomonas aeruginosa, and small blue copper proteins such as azurin and pseudoazurin. Cytochrome cd1 also has oxidase and hydroxylamine reductase activities. May also catalyse the reaction of hydroxylamine reductase (EC 1.7.99.1) since this is a well-known activity of cytochrome cd1.
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Word Map
- 1.7.2.1
- anemia
- mellitus
-
glycated
-
hematocrit
- erythrocyte
- hematological
- women
- arterial
-
glycemic
- transfusion
- platelet
- children
- albumin
- cardiovascular
- cholesterol
-
postoperative
- ferritin
- fetal
-
sickle
- creatinine
-
preoperative
- bleeding
- cardiac
- erythropoietin
- hypertension
- heme
- triglyceride
- hemorrhage
-
admission
-
systolic
- venous
-
demographic
-
january
-
hemolysis
-
c-reactive
-
erythroid
- hypoglycemia
-
comorbidities
- reticulocyte
-
hemodialysis
- transferrin
-
admitted
-
hemodynamic
-
placebo
-
diastolic
-
intraoperative
-
outpatient
-
anthropometric
- bilirubin
- waist
- medicine
- analysis
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
hemoglobin, cunir, dissimilatory nitrite reductase, marc2, marc1, pseudomonas cytochrome oxidase, cytochrome cd1 nitrite reductase, cu-nir, axnir, cytochrome cd, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cytochrome c-551:O2, NO2- oxidoreductase
-
-
-
-
cytochrome cd
cytochrome oxidase
-
-
-
-
oxidase, Pseudomonas cytochrome
-
-
-
-
Pseudomonas cytochrome oxidase
reductase, nitrite (cytochrome)
-
-
-
-
cytochrome cd
-
-
-
-
Pseudomonas cytochrome oxidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
electron transfer from c heme to d1 heme is very slow, order of seconds
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
electron-transfer mechanism
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
proposed reaction mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
nitric-oxide:ferricytochrome-c oxidoreductase
The reaction is catalysed by two types of enzymes, found in the perimplasm of denitrifying bacteria. One type comprises proteins containing multiple copper centres, the other a heme protein, cytochrome cd1. Acceptors include c-type cytochromes such as cytochrome c-550 or cytochrome c-551 from Paracoccus denitrificans or Pseudomonas aeruginosa, and small blue copper proteins such as azurin and pseudoazurin. Cytochrome cd1 also has oxidase and hydroxylamine reductase activities. May also catalyse the reaction of hydroxylamine reductase (EC 1.7.99.1) since this is a well-known activity of cytochrome cd1.
CAS REGISTRY NUMBER
COMMENTARY
9027-00-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nitric oxide + H2O + ferricytochrome c551
nitrite + ferrocytochrome c551 + H+
-
-
-
r
nitrite + electron donor
NO + oxidized electron donor + H2O
-
-
-
?
ferrocytochrome c-551 + NO2-
NO + ferricytochrome c-551
-
-
-
?
nitric oxide + H2O + ferricytochrome c
nitrite + ferrocytochrome c + H+
-
-
-
-
r
nitric oxide + H2O + ferricytochrome c551
nitrite + ferrocytochrome c551 + H+
-
-
-
-
r
nitrite + reduced ascorbate
nitric oxide + oxidized ascorbate
-
-
-
-
r
NO2- + ferrocytochrome c
NO + ferricytochrome c
-
probably most dominant activity in vivo
-
?
NO2- + morpholine
N-nitrosomorpholine
-
in the presence of diethyldithiocarbamic acid ethylester, nitrosation through the production of NO or NO+-like species
-
?
reduced azurin + O2
oxidized azurin + H2O
-
not known whether azurin donates electrons in vivo in parallel or sequentially to cytochrome c551
-
?
ferrocytochrome c-551 + O2
H2O + ferricytochrome c-551
-
inactive with eukaryotic cytochromes c
-
?
additional information
?
-
-
nitrite reductase from Pseudomonas aeruginosa released by antimicrobial agents and complement induces interleukin-8 production in bronchial epithelial cells
-
-
?
additional information
?
-
-
nitrite reductase in both oxidized and reduced states forms with NO two distinct compounds at both hemes. These compounds, in addition to the oxidized and reduced enzymes, are formed during the turnover of this enzyme as functional intermediates
-
-
?
additional information
?
-
-
spectroscopic analysis of the reactivity of cd1NiR and its semi-apo derivative with NO. The c heme nitrosylation is enhanced during catalysis
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NO2- + ferrocytochrome c
NO + ferricytochrome c
-
probably most dominant activity in vivo
-
?
reduced azurin + O2
oxidized azurin + H2O
-
not known whether azurin donates electrons in vivo in parallel or sequentially to cytochrome c551
-
?
additional information
?
-
-
nitrite reductase from Pseudomonas aeruginosa released by antimicrobial agents and complement induces interleukin-8 production in bronchial epithelial cells
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
characterization of the nitrosyl d1 heme complex by high-field-pulse electron papramagnetic spectroscopy spectra and derived 14N hyperfine and quadrupole interactions. Residue Y10 does not influence the NO ligand orientation in the reduced state in solution
heme d
-
oxidation-reduction behavior, formation of an oxygenated intermediate at heme d
-
Heme d1
-
the recombinant enzyme, expressed in Pseudomonas putida, contains c-heme but no d1-heme
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn
-
the recombinant enzyme, expressed in Pseudomonas putida, contains c-heme but no d1-heme. Reconstitution of this protein with Zn-protoporphyrin IX in the place of the d1-heme. Photoexcitation of Zn-NIR is followed by electron transfer from the triplet excited state of the Zn-porphyrin to the oxidized c-haem. Reduction of the d1-heme is associated with a substantial reorganization of the coordination of the metal
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
endogenous inhibitor of nitrite reductase from Pseudomonas aeruginosa: a non-blue copper-containing glycoprotein of 10000 Da that contains 1 atom of EPR-detectable type II copper
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Subtilisin
-
species of 48000 Da which contains the d1 but not the c heme
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0018
ferricytochrome c551
recombinant H327A mutant enzyme, O2 reduction
-
0.002
ferricytochrome c551
recombinant wild-type enzyme, O2 reduction
-
0.0075
ferricytochrome c551
recombinant H369A mutant enzyme, O2 reduction
-
0.0018
Ferrocytochrome c-551
pH 6.2, 25°C, mutant enzyme H327A
-
0.0075
Ferrocytochrome c-551
pH 6.2, 25°C, mutant enzyme H369A
-
0.035
azurin
-
recombinant wild-type and Y10F mutant enzyme, at pH 6.2 and 27°C
0.00177
ferricytochrome c551
-
recombinant wild-type enzyme, at pH 6.2 and 27°C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.032
Ferrocytochrome c-551
pH 6.2, 25°C, mutant enzyme H369A
-
0.043
Ferrocytochrome c-551
pH 6.2, 25°C, mutant enzyme H327A
-
0.583
ferricytochrome c551
-
recombinant wild-type enzyme, at pH 6.2 and 27°C
-
0.6
ferricytochrome c551
-
recombinant Y10F mutant enzyme, at pH 6.2 and 27°C
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
storage at -20°C for several months leads to an increase in the number of isoelectrophoretic forms. All preparations have two primary bands, one with a pI of 6.97 and the other of 7.02. Both bands possess significant cytochrome oxidase activity after elution from the gels. When each of the primary bands is eluted and again subject to isoelectric focusing under the same conditions as before, each band interconverts into two bands with pIs of 6.97 and 7.02
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the enzyme is synthesized exclusively in
additional information
-
enzyme is released from bacteria, after exposure to different antimicrobial agents
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme is released from bacteria, after exposure to different antimicrobial agents
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
-
enzyme NirS interacts with the potential haem d1 insertion protein NirN in vivo. This NirS-NirN interaction is dependent on the presence of the putative haem d1 biosynthesis enzyme NirF. NirS also directly interacts with NirF, a membrane anchored lipoprotein
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
model for the maturation of NirS in which the three proteins NirS, NirN and NirF form a transient, membrane-associated complex in order to achieve the last step of haem d1 biosynthesis and insertion of the cofactor haem d1 into NirS
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of the H327A mutant are obtained by vapor diffusion technique by mixing in a 1:1 ratio the protein and a reservoir solution containing 4.0% polyethylene glycol 5000 monomethyl ether, 0.1 M sodium acetate, pH 5.5. The space group is 4(3)22 with cell dimensions 70.5 x 70.5 x 281 A. Crystals of the H369A mutant are obtained by mixing in a 1.1 ratio the protein and a reservoir solution containing 11.5% polyethylene glycol 6000, 0.2 M imidazole/malate, pH 6.5. The space group is P4(1)2(1)2 with cell dimensions 94.7 x 94.7 x 159.9 A
H327A mutant enzymes: vapour diffusion technique, mixing of the enzyme and a reservoir solution containing 4% polyethylene glycol 5000 monomethyl ether, 100 mM sodium acetate pH 5.5 in a 1/1 ratio, H369A mutant enzyme: 11.5% polyethylene glycol 6000, 200 mM imidazole/malate pH 6.5, x-ray structure of both mutants
structure of the reduced enzyme both in the unbound form and with the physiological product, NO, bound at the d1 heme active site
crystals of the H327A mutants are obtained by vapour diffusion technique. Crystals of H369A are obtained by mixing equal volumes of a reservoir solution containing 11.5% PEG 6000, 0.2 M imidazole/malate, pH 6.5, and of protein, in presence or not of 50 mM potassium nitrite and 50 mM sodium ascorbate. Crystals belong to space group P4(1)2(1)2 with cell dimensions a = b = 94.7 A, c = 159.9 A. The three-dimensional structures of NIR mutant H327A, and H369A in complex with NO solved by multiple wave-length anomalous dispersion, using the iron anomalous signal, and molecular replacement techniques. In both refined crystal structures the c-heme domain, whilst preserving its classical c-type cytochrome fold, has undergone a 60° rigid-body rotation around an axis parallel with the pseudo 8-fold axis of the beta-propeller, and passing through residue Gln115. Even though the distance between the Fe ions of the c and d1-heme remains 21 A, the edge-to-edge distance between the two hemes has increased by 5 A. Furthermore the distal side of the d1-heme pocket appears to have undergone structural re-arrangement and Tyr10 has moved out of the active site. In the H369A-NO complex, the position and orientation of NO is significantly different from that of the NO bound to the reduced wild-type structure
-
the structure of the orthorhombic form (P2(1)2(1)2) of oxidized NiR-Pa is solved at 2.15 A resolution, using molecular replacement with the coordinates of the NiR from Thiosphaera pantotropha as the starting model
-
vapour diffusion at 20°C, in presence of 10% polyethylene glycol 4000, 50 mM Tris-HCl, pH 8.7, 400 mM NaCl, at a protein concentration of 14 mg/ml. The crystals are dark green elongated tetragonal prisms of dimensions 1.5 mm * 0.2 mm * 0.2 mm for the largest ones. These crystals are tetragonal with space group P4(1)(3)2(1)2 and cell dimensions a = b = 128.2 A, c = 172.6 A. They diffract at least up to 2.8 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H327A
H369A
H327A
-
the three-dimensional structures of NIR mutant H327A, and H369A in complex with NO solved by multiple wave-length anomalous dispersion, using the iron anomalous signal, and molecular replacement techniques. In both refined crystal structures the c-heme domain, whilst preserving its classical c-type cytochrome fold, has undergone a 60° rigid-body rotation around an axis parallel with the pseudo 8-fold axis of the beta-propeller, and passing through residue Gln115. Even though the distance between the Fe ions of the c and d1-heme remains 21 A, the edge-to-edge distance between the two hemes has increased by 5 A. Furthermore the distal side of the d1-heme pocket appears to have undergone structural re-arrangement and Tyr10 has moved out of the active site. In the H369A-NO complex, the position and orientation of NO is significantly different from that of the NO bound to the reduced wild-type structure
H369A
Y10F
H327A
mutant protein has no nitrite reductase activity but maintains the ability to reduce O2 to water. Nitrite reductase activity is impaired because of the accumulation of a catalytically inactive form
H369A
mutant protein has no nitrite reductase activity but maintains the ability to reduce O2 to water. Nitrite reductase activity is impaired because of the accumulation of a catalytically inactive form
H369A
-
the three-dimensional structures of NIR mutant H327A, and H369A in complex with NO solved by multiple wave-length anomalous dispersion, using the iron anomalous signal, and molecular replacement techniques. In both refined crystal structures the c-heme domain, whilst preserving its classical c-type cytochrome fold, has undergone a 60° rigid-body rotation around an axis parallel with the pseudo 8-fold axis of the beta-propeller, and passing through residue Gln115. Even though the distance between the Fe ions of the c and d1-heme remains 21 A, the edge-to-edge distance between the two hemes has increased by 5 A. Furthermore the distal side of the d1-heme pocket appears to have undergone structural re-arrangement and Tyr10 has moved out of the active site. In the H369A-NO complex, the position and orientation of NO is significantly different from that of the NO bound to the reduced wild-type structure
H369A
-
mutation impairs the reaction with O2, affecting both the properties and lifespan of the intermediate species
Y10F
-
no change in optical spectrum, nitrite and oxidase activity and heme c to heme d1 electron transfer rates compared to wild-type
Y10F
-
high-field-pulse electron papramagnetic spectroscopy spectra and the derived 14N hyperfine and quadrupole interactions are the same for wild-type and mutant. Residue Y10 does not influence the NO ligand orientation in the reduced state in solution
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
urea, 4 M, 9% of initial activity, 6 M, no dissociation into subunits but irreversible inactivation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, storage for several months leads to an increase in the number of isoelectrophoretic forms
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
monomeric enzyme prepared by controlled succinylation of the native dimer
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type, H327A and H369A mutant enzyme in Pseudomonas putida
expression of wild-type and Y10F mutant enzyme in Pseudomonas putida
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Silvestrini, M.C.; Falcinelli, S.; Ciabatti, I.; Cutruzzola, F.; Brunori, M.
Pseudomonas aeruginosa nitrite reductase (or cytochrome oxidase): an overview
Biochimie
76
641-654
1994
Alcaligenes faecalis, Paracoccus denitrificans, Halomonas halodenitrificans, Paracoccus pantotrophus, Pseudomonas aeruginosa, Pseudomonas stutzeri, Thiobacillus denitrificans
Silvestrini, M.C.; Tordi, M.G.; Citro, G.; Vecchini, P.; Brunori, M.
Monomeric Pseudomonas aeruginosa nitrite reductase: preparation, characterization, and kinetic properties
J. Inorg. Biochem.
57
169-181
1995
Pseudomonas aeruginosa
Yamazaki, T.; Oyanagi, H.; Fujiwara, T.; Fukumori, Y.
Nitrite reductase from the magnetotactic bacterium Magnetospirillum magnetotacticum. A novel cytochrome cd1 with Fe(II):nitrite oxidoreductase activity
Eur. J. Biochem.
233
665-671
1995
Magnetospirillum magnetotacticum, Pseudomonas aeruginosa
Schichman, S.A.; Meyer, T.E.; Gray, H.B.
Kinetics of electron transfer in Pseudomonas aeruginosa cytochrome cd1-nitrite reductase
Inorg. Chim. Acta
243
25-31
1996
Pseudomonas aeruginosa
-
Calmels, S.; Ohshima, H.; Henry, Y.; Bartsch, H.
Characterization of bacterial cytochrome cd(1)-nitrite reductase as one enzyme responsible for catalysis of nitrosation of secondary amines
Carcinogenesis
17
533-536
1996
Pseudomonas aeruginosa, Pseudomonas stutzeri
Cutruzzola, f.; Arese, M.; Grasso, S.; Bellelli, A.; Brunori, M.
Mutagenesis of nitrite reductase from Pseudomonas aeruginosa: tyrosine-10 in the c heme domain is not involved in catalysis
FEBS Lett.
412
365-369
1997
Pseudomonas aeruginosa
Ferguson, S.J.; Fulop, V.
Cytochrome cd1 nitrite reductase: structure raises interesting mechanistic questions
Subcell. Biochem.
35
519-540
2000
Paracoccus pantotrophus, Pseudomonas aeruginosa
Cutruzzola, F.; Brown, K.; Wilson, E.K.; Bellelli, A.; Arese, M.; Tegoni, M.
The nitrite reductase from Pseudomonas aeruginosa: essential role of two active-site histidines in the catalytic and structural properties
Proc. Natl. Acad. Sci. USA
98
2232-2237
2001
Pseudomonas aeruginosa (P24474)
Reutov, V.P.; Sorokina, E.G.
NO-Synthase and nitrite-reductase components of nitric oxide cycle
Biochemistry (Moscow)
63
874-884
1998
Paracoccus denitrificans, Pseudomonas aeruginosa
Arese, M.; Zumft, W.G.; Cutruzzola, F.
Expression of a fully functional cd1 nitrite reductase from Pseudomonas aeruginosa in Pseudomonas stutzeri
Protein Expr. Purif.
27
42-48
2003
Pseudomonas aeruginosa
Sar, B.; Oishi, K.; Wada, A.; Hirayama, T.; Matsushima, K.; Nagatake, T.
Nitrite reductase from Pseudomonas aeruginosa released by antimicrobial agents and complement induces interleukin-8 production in bronchial epithelial cells
Antimicrob. Agents Chemother.
43
794-801
1999
Pseudomonas aeruginosa, Pseudomonas aeruginosa 5276
Hull, H.H.; Wharton, D.C.
Isoelectrophoretic characterization of Pseudomonas cytochrome oxidase/nitrite reductase and its heme d1-containing domain
Arch. Biochem. Biophys.
301
85-90
1993
Pseudomonas aeruginosa
Silvestrini, M.C.; Cutruzzola, F.; D'Alessandro, R.; Brunori, M.; Fochesato, N.; Zennaro, E.
Expression of Pseudomonas aeruginosa nitrite reductase in Pseudomonas putida and characterization of the recombinant protein
Biochem. J.
285
661-666
1992
Pseudomonas aeruginosa
Bellelli, A.; Brzezinski, P.; Arese, M.; Cutruzolla, F.; Silvestrini, M.C.
Electron transfer in zinc-reconstituted nitrite reductase from Pseudomonas aeruginosa
Biochem. J.
319
407-410
1996
Pseudomonas aeruginosa
-
Nurizzo, D.; Cutruzzola, F.; Arese, M.; Bourgeois, D.; Brunori, M.; Cambillau, C.; Tegoni, M.
Conformational changes occurring upon reduction and NO binding in nitrite reductase from Pseudomonas aeruginosa
Biochemistry
37
13987-13996
1998
Pseudomonas aeruginosa (P24474), Pseudomonas aeruginosa
Karapetian, A.V.; Kamalian, M.G.; Nalbandyan, R.M.
A copper-containing protein that inhibits nitrite reductase from Pseudomonas aeruginosa
FEBS Lett.
203
131-134
1986
Pseudomonas aeruginosa
Shimada, H.; Orii, Y.
The nitric oxide compounds of Pseudomonas aeruginosa nitrite reductase and their probable participation in the nitrite reduction
FEBS Lett.
54
237-240
1975
Pseudomonas aeruginosa
Coyne, M.S.; Arunakumari, A.; Pankratz, H.S.; Tiedje, J.M.
Localization of the cytochrome cd1 and copper nitrite reductases in denitrifying bacteria
J. Bacteriol.
172
2558-2562
1990
Pseudomonas aeruginosa, Pseudomonas fluorescens
Shimada, H.; Orii, Y.
Oxidation-reduction behavior of the heme c and heme d moieties of Pseudomonas aeruginosa nitrite reductase and the formation of an oxygenated intermediate at heme d1
J. Biochem.
80
135-140
1976
Pseudomonas aeruginosa
Shimada, H.; Orii, Y.
The pH-dependent reactions of Pseudomonas aeruginosa nitrite reductase with nitric oxide and nitrite
J. Biochem.
84
1553-1558
1978
Pseudomonas aeruginosa
Yap-Bondoc, F.; Timkovich, R.
Inactivation of cytochrome cd1 by hydrazines
J. Biol. Chem.
265
4247-4253
1990
Pseudomonas aeruginosa
Takano, T.; Dickerson, R.E.; Schichman, S.A.; Meyer, T.E.
Crystal data, molecular dimensions and molecular symmetry in cytochrome oxidase from Pseudomonas aeruginosa
J. Mol. Biol.
133
185-188
1979
Pseudomonas aeruginosa
Tegoni, M.; Silvestrini, M.C.; Lamzin, V.S.; Brunori, M.; Cambillau, C.
Crystallization and preliminary X-ray analysis of a new crystal form of nitrite reductase from Pseudomonas aeruginosa
J. Mol. Biol.
243
347-350
1994
Pseudomonas aeruginosa
Brown, K.; Roig-Zamboni, V.; Cutruzzola, F.; Arese, M.; Sun, W.; Brunori, M.; Cambillau, C.; Tegoni, M.
Domain swing upon His to Ala mutation in nitrite reductase of Pseudomonas aeruginosa
J. Mol. Biol.
312
541-554
2001
Pseudomonas aeruginosa
Nurizzo, D.; Silvestrini, M.C.; Mathieu, M.; Cutruzzola, F.; Bourgeois, D.; Fulop, V.; Hajdu, J.; Brunori, M.; Tegoni, M.; Cambillau, C.
N-terminal arm exchange is observed in the 2.15 A crystal structure of oxidized nitrite reductase from Pseudomonas aeruginosa
Structure
5
1157-1171
1997
Pseudomonas aeruginosa
Centola, F.; Rinaldo, S.; Brunori, M.; Cutruzzola, F.
Critical role of His369 in the reactivity of Pseudomonas aeruginosa cytochrome cd1 nitrite reductase with oxygen
FEBS J.
273
4495-4503
2006
Pseudomonas aeruginosa
Radoul, M.; Centola, F.; Rinaldo, S.; Cutruzzola, F.; Pecht, I.; Goldfarb, D.
Heme d1 nitrosyl complex of cd1 nitrite reductase studied by high-field-pulse electron paramagnetic resonance spectroscopy
Inorg. Chem.
48
3913-3915
2009
Pseudomonas aeruginosa
Nicke, T.; Schnitzer, T.; Muench, K.; Adamczack, J.; Haufschildt, K.; Buchmeier, S.; Kucklick, M.; Felgentraeger, U.; Jaensch, L.; Riedel, K.; Layer, G.
Maturation of the cytochrome cd1 nitrite reductase NirS from Pseudomonas aeruginosa requires transient interactions between the three proteins NirS, NirN and NirF
Biosci. Rep.
33
e00048
2013
Pseudomonas aeruginosa
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