The key role of water in the dioxygenase function of Escherichia coli flavohemoglobin
Flavohemoglobins (FHbs) are members of the globin superfamily, widely distributed among
prokaryotes and eukaryotes that have been shown to carry out nitric oxide dioxygenase …
prokaryotes and eukaryotes that have been shown to carry out nitric oxide dioxygenase …
[HTML][HTML] Allostery in the nitric oxide dioxygenase mechanism of flavohemoglobin
AM Gardner, PR Gardner - Journal of Biological Chemistry, 2021 - ASBMB
The substrates O 2 and NO cooperatively activate the NO dioxygenase function of
Escherichia coli flavohemoglobin. Steady-state and transient kinetic measurements support …
Escherichia coli flavohemoglobin. Steady-state and transient kinetic measurements support …
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˙ …
enzymes against NO˙‐mediated toxicity. FlavoHbs dominantly function as an NO˙ …
[PDF][PDF] Unusual structure of the oxygen-binding site in the dimeric bacterial hemoglobin from Vitreoscilla sp
C Tarricone, A Galizzi, A Coda, P Ascenzi, M Bolognesi - Structure, 1997 - cell.com
Background: The first hemoglobin identified in bacteria was isolated from Vitreoscilla
stercoraria (VtHb) as a homodimeric species. The wild-type protein has been reported to …
stercoraria (VtHb) as a homodimeric species. The wild-type protein has been reported to …
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 …
reductaselike FAD‐and NAD‐binding modules. These proteins are widely represented …
Structure of Ralstonia eutropha Flavohemoglobin in Complex with Three Antibiotic Azole Compounds
E El Hammi, E Warkentin, U Demmer, F Limam… - Biochemistry, 2011 - ACS Publications
Flavohemoglobins (flavoHbs) are enzymes that operate primarily as nitric oxide
dioxygenases and shuttle thereby electrons among NAD (P) H, FAD, heme, and a ligated …
dioxygenases and shuttle thereby electrons among NAD (P) H, FAD, heme, and a ligated …
[HTML][HTML] Flavohemoglobin, a globin with a peroxidase-like catalytic site
M Mukai, CE Mills, RK Poole, SR Yeh - Journal of Biological Chemistry, 2001 - ASBMB
Biochemical studies of flavohemoglobin (Hmp) from Escherichia coli suggest that instead of
aerobic oxygen delivery, a dioxygenase converts NO to NO 3− and anaerobically, an NO …
aerobic oxygen delivery, a dioxygenase converts NO to NO 3− and anaerobically, an NO …
Antimicrobial agents act differently on Staphyloccocus aureus and Ralstonia eutropha flavohemoglobins
A Ezzine, M Moussaoui, E El Hammi… - Applied biochemistry …, 2014 - Springer
Flavohemoglobins (FlavoHb) play a key role in bacterial resistance to nitrosative stress and
NO signaling modulation. In this study, we cloned, expressed, and characterized the flavoHb …
NO signaling modulation. In this study, we cloned, expressed, and characterized the flavoHb …
[HTML][HTML] Unusual heme iron-lipid acyl chain coordination in Escherichia coli flavohemoglobin
P D'Angelo, D Lucarelli, S Della Longa, M Benfatto… - Biophysical journal, 2004 - cell.com
Escherichia coli flavohemoglobin is endowed with the notable property of binding
specifically unsaturated and/or cyclopropanated fatty acids both as free acids or …
specifically unsaturated and/or cyclopropanated fatty acids both as free acids or …