Flavohemoglobin: structure and reactivity

A Bonamore, A Boffi - IUBMB life, 2008 - Wiley Online Library
Flavohemoglobins (flavoHbs) are made of a globin domain fused with a ferredoxin
reductaselike FAD‐and NAD‐binding modules. These proteins are widely represented …

Protection from nitrosative stress: a central role for microbial flavohemoglobin

MT Forrester, MW Foster - Free Radical Biology and Medicine, 2012 - Elsevier
Nitric oxide (NO) is an inevitable product of life in an oxygen-and nitrogen-rich environment.
This reactive diatomic molecule exhibits microbial cytotoxicity, in large part by facilitating …

Flavohemoglobin Hmp, but not its individual domains, confers protection from respiratory inhibition by nitric oxide in Escherichia coli

E Hernández-Urzua, CE Mills, GP White… - Journal of Biological …, 2003 - ASBMB
Escherichia coli possesses a two-domain flavohemoglobin, Hmp, implicated in nitric oxide
(NO) detoxification. To determine the contribution of each domain of Hmp toward NO …

[HTML][HTML] Flavohaemoglobin: The pre-eminent nitric oxide–detoxifying machine of microorganisms

RK Poole - F1000Research, 2020 - ncbi.nlm.nih.gov
Flavohaemoglobins were first described in yeast as early as the 1970s but their functions
were unclear. The surge in interest in nitric oxide biology and both serendipitous and …

Escherichia coli flavohemoglobin is an efficient alkylhydroperoxide reductase

A Bonamore, P Gentili, A Ilari, ME Schinina… - Journal of Biological …, 2003 - ASBMB
Escherichia coli flavohemoglobin (HMP) is shown to be capable of catalyzing the reduction
of several alkylhydroperoxide substrates into their corresponding alcohols using NADH as …

New functions for the ancient globin family: bacterial responses to nitric oxide and nitrosative stress: MicroReview

RK Poole, MN Hughes - Molecular Microbiology, 2000 - Wiley Online Library
Globin‐like oxygen‐binding proteins occur in bacteria, yeasts and other fungi, and protozoa.
The simplest contain protohaem as sole prosthetic group, but show considerable variation in …

Chimeric Vitreoscilla Hemoglobin (VHb) Carrying a Flavoreductase Domain Relieves Nitrosative Stress in Escherichia coli: New Insight into the Functional Role of …

R Kaur, R Pathania, V Sharma… - Applied and …, 2002 - Am Soc Microbiol
Dimeric hemoglobin (VHb) from the bacterium Vitreoscilla sp. strain C1 displays 30 to 53%
sequence identity with the heme-binding domain of flavohemoglobins (flavoHbs) and …

Active site analysis of yeast flavohemoglobin based on its structure with a small ligand or econazole

E El Hammi, E Warkentin, U Demmer… - The FEBS …, 2012 - Wiley Online Library
Flavohemoglobins (flavoHbs) serve various microorganisms as the major protective
enzymes against NO˙‐mediated toxicity. FlavoHbs dominantly function as an NO˙ …

Role for the Salmonella flavohemoglobin in protection from nitric oxide

MJ Crawford, DE Goldberg - Journal of Biological Chemistry, 1998 - ASBMB
Hemoglobin homologs are being identified in an expanding number of unicellular
prokaryotic and eukaryotic organisms. Many of these hemoglobins are twodomain proteins …

Protection from nitrosative stress by yeast flavohemoglobin

L Liu, M Zeng, A Hausladen… - Proceedings of the …, 2000 - National Acad Sciences
Yeast hemoglobin was discovered close to half a century ago, but its function has remained
unknown. Herein, we report that this flavohemoglobin protects Saccharomyces cerevisiae …