Reactome | CYGB dioxygenates NO

CYGB dioxygenates NO

Stable Identifier

R-HSA-5340226

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol

Synonyms

Fe(II)-heme b-(protein) + nitric oxide + O2 => Fe(III)-heme b-(protein) + nitrate

ReviewStatus

5/5

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Cytosolic cytoglobin dimer, CYGB(Fe2+) catalyzes the reaction of O2 and NO to form NO3, converting CYBG(Fe2+) to CYBG(Fe3+) in the process (Gardner 2005; Gardner et al. 2010; Hamdane et al. 2003). For CYBG to function catalytically, its associated Fe3+ must be reduced to Fe2+ (Smagghe et al. 2008). This reduction can be efficiently mediated by ascorbate (Liu et al. 2013) and by CYB5B (cytochrome b5 type B) in vitro (Amdahl et al. 2017). The molecular details of the physiological reduction process remain unclear, so these entities are annotated as positive regulators of the dioxygenation reaction catalyzed by CYGB.

Literature References

PubMed ID	Title	Journal	Year
19147491	Cytoglobin is expressed in the vasculature and regulates cell respiration and proliferation via nitric oxide dioxygenation Halligan, KE, Jourd'heuil, FL, Jourd'heuil, D	J. Biol. Chem.	2009
14530264	The redox state of the cell regulates the ligand binding affinity of human neuroglobin and cytoglobin Hamdane, D, Kiger, L, Dewilde, S, Green, BN, Pesce, A, Uzan, J, Burmester, T, Hankeln, T, Bolognesi, M, Moens, L, Marden, MC	J. Biol. Chem.	2003
23710929	Differences in oxygen-dependent nitric oxide metabolism by cytoglobin and myoglobin account for their differing functional roles Liu, X, Tong, J, Zweier, JR, Follmer, D, Hemann, C, Ismail, RS, Zweier, JL	FEBS J	2013
11893755	A ubiquitously expressed human hexacoordinate hemoglobin Trent, JT, Hargrove, MS	J. Biol. Chem.	2002
20511233	Nitric-oxide dioxygenase function of human cytoglobin with cellular reductants and in rat hepatocytes Gardner, AM, Cook, MR, Gardner, PR	J Biol Chem	2010
28671819	Efficient Reduction of Vertebrate Cytoglobins by the Cytochrome b₅/Cytochrome b₅ Reductase/NADH System Amdahl, MB, Sparacino-Watkins, CE, Corti, P, Gladwin, MT, Tejero, J	Biochemistry	2017
18446211	NO dioxygenase activity in hemoglobins is ubiquitous in vitro, but limited by reduction in vivo Smagghe, BJ, Trent JT, 3rd, Hargrove, MS	PLoS One	2008
15598505	Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases Gardner, PR	J. Inorg. Biochem.	2005