MF_01252

Flavohemoprotein [hmp]

HAMAP entry
Member databaseHAMAP
HAMAP typefamily
Short nameHmp

Description
Imported from IPR023950

This entry represents flavohemoproteins, which have multiple enzymatic activities and consist of three distinct domains - an N-terminal heme- and oxygen-binding domain (globin domain) followed by an oxidoreductase FAD-binding domain and a NAD-binding reductase domain
[7, 8]
. They function as nitric oxide dioxygenases
[6]
and a ferrisiderophore reductase whereby the complexed Fe+3 iron of siderophores are reduced to Fe+2 and released
[2, 3, 4, 5]
. They are involved in the inducible response to nitrosative stress, as their nitric oxide dioxygenase ability is used in aerobic NO detoxification, a reaction which utilises O2 and NAD(P)H to convert NO to nitrate and therefore offers protection from various noxious nitrogen compounds
[1]
.

References
Imported from IPR023950

1.Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon monoxide inhibition. Gardner PR, Gardner AM, Martin LA, Dou Y, Li T, Olson JS, Zhu H, Riggs AF. J. Biol. Chem. 275, 31581-7, (2000). View articlePMID: 10922365

2.Steady-state and transient kinetics of Escherichia coli nitric-oxide dioxygenase (flavohemoglobin). The B10 tyrosine hydroxyl is essential for dioxygen binding and catalysis. Gardner AM, Martin LA, Gardner PR, Dou Y, Olson JS. J. Biol. Chem. 275, 12581-9, (2000). View articlePMID: 10777548

3.Nitric oxide dioxygenase: an enzymic function for flavohemoglobin. Gardner PR, Gardner AM, Martin LA, Salzman AL. Proc. Natl. Acad. Sci. U.S.A. 95, 10378-83, (1998). View articlePMID: 9724711

4.The haemoglobin-like protein (HMP) of Escherichia coli has ferrisiderophore reductase activity and its C-terminal domain shares homology with ferredoxin NADP+ reductases. Andrews SC, Shipley D, Keen JN, Findlay JB, Harrison PM, Guest JR. FEBS Lett. 302, 247-52, (1992). View articlePMID: 1601132

5.Reactions of the Escherichia coli flavohaemoglobin (Hmp) with oxygen and reduced nicotinamide adenine dinucleotide: evidence for oxygen switching of flavin oxidoreduction and a mechanism for oxygen sensing. Poole RK, Ioannidis N, Orii Y. Proc. Biol. Sci. 255, 251-8, (1994). PMID: 8022841

6.Flavohemoglobin detoxifies nitric oxide in aerobic, but not anaerobic, Escherichia coli. Evidence for a novel inducible anaerobic nitric oxide-scavenging activity. Gardner AM, Gardner PR. J. Biol. Chem. 277, 8166-71, (2002). View articlePMID: 11751864

7.Structure of Ralstonia eutropha flavohemoglobin in complex with three antibiotic azole compounds. El Hammi E, Warkentin E, Demmer U, Limam F, Marzouki NM, Ermler U, Baciou L. Biochemistry 50, 1255-64, (2011). View articlePMID: 21210640

8.The X-ray structure of ferric Escherichia coli flavohemoglobin reveals an unexpected geometry of the distal heme pocket. Ilari A, Bonamore A, Farina A, Johnson KA, Boffi A. J. Biol. Chem. 277, 23725-32, (2002). View articlePMID: 11964402

This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.