Impact of azole drugs on energetics, kinetics, and ligand migration pathways of CO photo-dissociation in bacterial flavohemoglobins
D Butcher, M Moussaoui, L Baciou, J Miksovska - RSC advances, 2020 - pubs.rsc.org
Flavohemoglobins (fHbs) are heme proteins found in prokaryotic and eukaryotic microbes.
They are involved in NO detoxification through an NO˙ dioxygenase mechanism. The N …
They are involved in NO detoxification through an NO˙ dioxygenase mechanism. The N …
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 …
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 …
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 …
Resonance Raman studies on the flavohemoglobin of the protist Giardia intestinalis: evidence of a type I/II-peroxidase-like heme environment and roles of the active …
B Lukaszewicz, E McColl, J Yee, S Rafferty… - JBIC Journal of …, 2017 - Springer
Flavohemoglobins are microbial enzymes that counter nitrosative stress, but the details of
their underlying enzymatic activities and structure–function relationships are not completely …
their underlying enzymatic activities and structure–function relationships are not completely …
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˙ …
New insights into the mechanism of electron transfer within flavohemoglobins: tunnelling pathways, packing density, thermodynamic and kinetic analyses
E El Hammi, C Houée-Lévin, J Řezáč, B Lévy… - Physical Chemistry …, 2012 - pubs.rsc.org
Flavohemoglobins (FlavoHb) are metalloenzymes catalyzing the reaction of nitric oxide
dioxygenation. The iron cation of the heme group needs to be preliminarily reduced to the …
dioxygenation. The iron cation of the heme group needs to be preliminarily reduced to the …
Type II flavohemoglobin of Mycobacterium smegmatis oxidizes d-lactate and mediate electron transfer
Two distantly related flavohemoglobins (FHbs), MsFHbI and Ms FHbII, having crucial
differences in their heme and reductase domains, co-exist in Mycobacterium smegmatis …
differences in their heme and reductase domains, co-exist in Mycobacterium smegmatis …
An unconventional hexacoordinated flavohemoglobin from Mycobacterium tuberculosis
Being an obligate aerobe, Mycobacterium tuberculosis faces a number of energetic
challenges when it encounters hypoxia and environmental stress during intracellular …
challenges when it encounters hypoxia and environmental stress during intracellular …
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 …