Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search General Information

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 10 of 12 > >>
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.7.2.2evolution the enzyme is a member of the multiheme cytochrome c family. Members of the Hao subfamily, here called epilonHao proteins, have been predicted from the genomes of nitrate/nitrite-ammonifying bacteria that usually lack NrfA. Formation of a membrane-bound HaoCA assembly reminiscent of the menaquinol-oxidizing NrfHA complex. epsilonHao proteins form a subfamily of ammonifying cytochrome c nitrite reductases that represents a missing link in the evolution of NrfA, EC 1.7.2.2, and Hao, EC 1.7.99.1, enzymes, epsilonHao-type proteins are ancestors of different multiheme cytochrome c (MCC) subfamilies that catalyze either reductive (NrfA-type MCCs) or oxidative (Hao/Hdh-type MCCs) reactions. Comparison of the enzyme from Caminibacter mediatlanticus with NrfA from Wolinella succinogenes and Hao from Nitrosomonas europaea, overview 743303
Display the word mapDisplay the reaction diagram Show all sequences 1.7.2.2evolution the enzyme is a member of the multiheme cytochrome c family. Members of the Hao subfamily, here called epilonHao proteins, have been predicted from the genomes of nitrate/nitrite-ammonifying bacteria that usually lack NrfA. Formation of a membrane-bound HaoCA assembly reminiscent of the menaquinol-oxidizing NrfHA complex. epsilonHao proteins form a subfamily of ammonifying cytochrome c nitrite reductases that represents a missing link in the evolution of NrfA, EC 1.7.2.2, and Hao, EC 1.7.99.1, enzymes, epsilonHao-type proteins are ancestors of different multiheme cytochrome c (MCC) subfamilies that catalyze either reductive (NrfA-type MCCs) or oxidative (Hao/Hdh-type MCCs) reactions. Comparison of the enzyme from Campylobacter curvus with NrfA from Wolinella succinogenes and Hao from Nitrosomonas europaea, overview 743303
Display the word mapDisplay the reaction diagram Show all sequences 1.7.2.2evolution the enzyme is a member of the multiheme cytochrome c family. Members of the Hao subfamily, here called epilonHao proteins, have been predicted from the genomes of nitrate/nitrite-ammonifying bacteria that usually lack NrfA. Formation of a membrane-bound HaoCA assembly reminiscent of the menaquinol-oxidizing NrfHA complex. epsilonHao proteins form a subfamily of ammonifying cytochrome c nitrite reductases that represents a missing link in the evolution of NrfA, EC 1.7.2.2, and Hao, EC 1.7.99.1, enzymes, epsilonHao-type proteins are ancestors of different multiheme cytochrome c (MCC) subfamilies that catalyze either reductive (NrfA-type MCCs) or oxidative (Hao/Hdh-type MCCs) reactions. Comparison of the enzyme from Campylobacter fetus with NrfA from Wolinella succinogenes and Hao from Nitrosomonas europaea, overview 743303
Display the word mapDisplay the reaction diagram Show all sequences 1.7.2.2evolution the enzyme is a member of the multiheme cytochrome c family. Members of the Hao subfamily, here called epilonHao proteins, have been predicted from the genomes of nitrate/nitrite-ammonifying bacteria that usually lack NrfA. Formation of a membrane-bound HaoCA assembly reminiscent of the menaquinol-oxidizing NrfHA complex. epsilonHao proteins form a subfamily of ammonifying cytochrome c nitrite reductases that represents a missing link in the evolution of NrfA, EC 1.7.2.2, and Hao, EC 1.7.99.1, enzymes, epsilonHao-type proteins are ancestors of different multiheme cytochrome c (MCC) subfamilies that catalyze either reductive (NrfA-type MCCs) or oxidative (Hao/Hdh-type MCCs) reactions. Comparison of the enzyme from Nautilia profundicola with NrfA from Wolinella succinogenes and Hao from Nitrosomonas europaea, overview 743303
Display the word mapDisplay the reaction diagram Show all sequences 1.7.2.2metabolism nitrite-loaded ccNiR is reduced in a concerted two-electron step to generate an [FeNO]7 moiety at the active site, with an associated midpoint potential of +246 mV vs standard hydrogen electrode at pH 7. Cyanide-bound active site reduction is a one-electron process with a midpoint potential of +20 mV, and without a strong-field ligand the active site midpoint potential shifts 70 mV lower still. The [FeNO]7 moiety possesses an spectral signature, different from those normally observed for [FeNO]7 hemes, that may indicate magnetic interaction of the active site with nearby hemes. Catalytic nitrite reduction to ammonia by ccNiR requires an applied potential of at least -120 mV, well below the midpoint potential for [FeNO]7 formation 764971
Display the word mapDisplay the reaction diagram Show all sequences 1.7.2.2metabolism reduction of nitrite-loaded ccNiR by N,N,N',N'-tetramethyl-pphenylenediamine generates a transient intermediate, identified as FeH1II(NO2-), where FeH1 represents the ccNiR active site. FeH1II(NO2-) accumulates rapidly and is then more slowly converted to the two-electron-reduced moiety [FeH1NO]7. ccNiR is not reduced beyond the [FeH1NO]7 state. The midpoint potentials for sequential reduction of FeH1III(NO2-) to FeH1II(NO2-) and then to [FeH1NO]7 are 130 and 370 mV versus the standard hydrogen electrode, respectively. With weak reductants, free NO radical is released from nitrite-loaded ccNiR 764182
Display the word mapDisplay the reaction diagram Show all sequences 1.7.2.2metabolism three-step nitrite reduction cycle on a dinuclear ruthenium platform [(HB(pyrazol-1-yl)3Ru)2(my-pz)] producing ammonia. The cycle comprises conversion of a nitrito ligand to a NO ligand using 2H+ and e-, subsequent reduction of the NO ligand to a nitrido and a H2O ligand by consumption of 2H+ and 5e-, and recovery of the parent nitrito ligand. Release of ammonia is detected 764970
Display the word mapDisplay the reaction diagram Show all sequences 1.7.2.2more comparison of reaction mechanisms of nitrogenase, EC 1.18.6.1, and multiheme cytochrome c nitrite reductase, ccNIR, EC 1.7.2.2, overview 742740
Display the word mapDisplay the reaction diagram Show all sequences 1.7.2.2physiological function ammonium-producing nitrite reductase NirBD is involved in regulating NO homeostasis. NirBD clears the accumulated nitrite from the medium. Nir deletion mutants show increased NO-dependent gene expression at later culture stages, whereas the wild-type M145 shows decreased expression. The nir deletion mutant produces more red-pigmented antibiotic than that produced by the wild-type -, 764682
Display the word mapDisplay the reaction diagram Show all sequences 1.7.2.2physiological function gene SO0265 encodes CcmI, an apocytochrome c chaperone, that is important and essential for maturation of c-type cytochromes with the canonical heme binding motif(s) (HBM and CX2CH) and nitrite reductase NrfA carrying a non-canonical CX2CK motif, respectively. The N-terminal transmembrane segment of CcmI, CcmI-1, is sufficient for maturation of the former but the entire protein is required for maturation of the latter. SirE is not required for maturation of NrfA 743309
Results 1 - 10 of 12 > >>