Theoretical insight into the hydroxylamine oxidoreductase mechanism

Fernandez, M.L.; Estrin, D.A.; Bari, S.E.; J. Inorg. Biochem. 102, 1523-1530 (2008)

Data extracted from this reference:

Metals/Ions

Metals/Ions	Commentary	Organism	Structure
Fe2+	as Fe(II)NO in the c-type heme	Nitrosomonas europaea

Organism

Organism	Primary Accession No. (UniProt)	Commentary	Textmining
Nitrosomonas europaea	-	-	-

Reaction

Reaction	Commentary	Organism
hydroxylamine + NH3 + acceptor = N2 + H2O + reduced acceptor	the meso tyrosyl residue enhances the binding of hydroxylamine, and increases the stability of a FeIIINO intermediate, while behaving indifferently in the FeIINO form, catalytic mechanism, modelling, overview	Nitrosomonas europaea

Substrates and Products (Substrate)

Substrates	Commentary Substrates	Literature (Substrates)	Organism	Products	Commentary (Products)	Literature (Products)	Organism (Products)	Reversibility
More	the enzyme catalyzes the conversion of hydroxylamine to nitrite, with a complicate arrangement of heme groups in three subunits	699386	Nitrosomonas europaea	?	-	-	-	-

Subunits

Subunits	Commentary	Organism
trimer	complicate arrangement of heme groups in three subunits. As a distinctive feature, the protein has a covalent linkage between a tyrosyl residue of one subunit and a meso carbon atom of the heme active site of another	Nitrosomonas europaea

Cofactor

Cofactor	Commentary	Organism	Structure
cytochrome P460	cytochrome P460 heme, c-type heme, and planar heme, structure modelling, overview	Nitrosomonas europaea	-

Cofactor (protein specific)

Cofactor	Commentary	Organism	Structure
cytochrome P460	cytochrome P460 heme, c-type heme, and planar heme, structure modelling, overview	Nitrosomonas europaea	-

Metals/Ions (protein specific)

Metals/Ions	Commentary	Organism	Structure
Fe2+	as Fe(II)NO in the c-type heme	Nitrosomonas europaea

Substrates and Products (Substrate) (protein specific)

Substrates	Commentary Substrates	Literature (Substrates)	Organism	Products	Commentary (Products)	Literature (Products)	Organism (Products)	Reversibility
More	the enzyme catalyzes the conversion of hydroxylamine to nitrite, with a complicate arrangement of heme groups in three subunits	699386	Nitrosomonas europaea	?	-	-	-	-

Subunits (protein specific)

Subunits	Commentary	Organism
trimer	complicate arrangement of heme groups in three subunits. As a distinctive feature, the protein has a covalent linkage between a tyrosyl residue of one subunit and a meso carbon atom of the heme active site of another	Nitrosomonas europaea

See also following references to EC number 1.7.99.8 (sorted by year of publication):

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)
710728	Cedervall		Crystallization and preliminar ...	Nitrosomonas europaea	Acta Crystallogr. Sect. F	65	1296-1298	2009	-	-	-	1	-	-	-	-	-	-	-	1	-	1	-	-	1	-	-	-	-	-	1	1	-	-	-	-	-	-	-	1	-	-	-	-	-	-	1	1	-	-	-	-	-	-	-	-	-	1	-	-	-	1	-	-	-	-	1	1	-	-	-	-	-	-	-	-	-	-	-	-	-	-
699009	Kostera		Kinetic and product distributi ...	Nitrosomonas europaea	J. Biol. Inorg. Chem.	13	1073-1083	2008	-	-	-	-	-	-	-	1	-	-	-	1	-	1	-	-	-	1	-	-	-	-	3	1	-	-	-	-	-	-	-	3	-	-	-	-	-	-	3	-	-	-	-	-	-	1	-	-	-	1	-	-	-	-	-	-	-	-	3	1	-	-	-	-	-	-	-	-	-	-	-	-	-	-
699041	Shimamura		Another multiheme protein, hyd ...	planctomycete KSU-1	J. Biosci. Bioeng.	105	243-248	2008	-	-	1	-	-	-	-	2	-	-	1	1	-	6	-	-	1	-	-	-	1	-	7	1	2	-	1	-	2	-	1	4	-	-	-	-	-	1	6	-	-	-	-	-	-	2	-	-	1	1	-	-	-	2	-	-	2	-	7	1	2	-	1	-	2	-	1	-	-	-	-	-	-	-
699386	Fernandez		Theoretical insight into the h ...	Nitrosomonas europaea	J. Inorg. Biochem.	102	1523-1530	2008	-	-	-	-	-	-	-	-	-	1	-	-	-	1	-	-	-	1	-	-	-	-	1	1	-	-	-	-	-	-	-	1	-	-	-	-	-	-	1	-	-	-	-	-	-	-	-	1	-	-	-	-	-	-	-	-	-	-	1	1	-	-	-	-	-	-	-	-	-	-	-	-	-	-
695734	Shimamura		Isolation of a multiheme prote ...	planctomycete KSU-1	Appl. Environ. Microbiol.	73	1065-1072	2007	-	-	1	-	-	-	2	1	-	-	1	1	-	4	-	-	1	-	-	-	1	-	7	1	1	-	-	-	1	-	1	1	1	-	-	-	-	1	1	-	-	-	-	2	1	1	-	-	1	1	-	-	-	1	-	-	1	-	7	1	1	-	-	-	1	-	1	-	-	-	-	-	-	-
696141	Jetten		1994-2004: 10 years of researc ...	Candidatus Brocadia anammoxidans, Candidatus Kuenenia stuttgartiensis, Candidatus Scalindua brodae	Biochem. Soc. Trans.	33	119-123	2005	-	3	-	-	-	-	-	-	3	-	-	3	-	7	-	-	-	-	-	-	-	-	3	-	-	-	-	-	-	-	-	-	-	-	-	-	3	-	-	-	-	-	-	-	-	-	3	-	-	3	-	-	-	-	-	-	-	-	3	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-
697514	Jetten		Microbiology and application o ...	Candidatus Brocadia anammoxidans, Candidatus Kuenenia stuttgartiensis	Curr. Opin. Biotechnol.	12	283-288	2001	-	2	-	-	-	-	-	-	2	-	-	2	-	2	-	-	-	-	-	-	-	-	2	-	-	-	-	-	-	-	-	-	-	-	-	-	2	-	-	-	-	-	-	-	-	-	2	-	-	2	-	-	-	-	-	-	-	-	2	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-
394344	Schalk		Involvement of a novel hydroxy ...	Candidatus Brocadia anammoxidans	Biochemistry	39	5405-5412	2000	-	-	-	-	-	-	5	3	-	-	2	1	-	1	-	-	1	-	-	-	-	-	10	1	2	-	-	-	1	-	-	1	-	1	-	-	-	-	1	-	-	-	-	5	-	3	-	-	2	1	-	-	-	1	-	-	-	-	10	1	2	-	-	-	1	-	-	1	-	-	-	-	-	-