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˙ …
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 …
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 …
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] Nitric-oxide dioxygenase activity and function of flavohemoglobins: sensitivity to nitric oxide and carbon monoxide inhibition
PR Gardner, AM Gardner, LA Martin, Y Dou, T Li… - Journal of Biological …, 2000 - ASBMB
Widely distributed flavohemoglobins (flavoHbs) function as NO dioxygenases and confer
upon cells a resistance to NO toxicity. FlavoHbs from Saccharomyces cerevisiae …
upon cells a resistance to NO toxicity. FlavoHbs from Saccharomyces cerevisiae …
Cloning and characterization of two flavohemoglobins from Aspergillus oryzae
S Zhou, S Fushinobu, Y Nakanishi, SW Kim… - Biochemical and …, 2009 - Elsevier
Two flavohemoglobin (FHb) genes, fhb1 and fhb2, were cloned from Aspergillus oryzae. The
amino acid sequences of the deduced FHb1 and FHb2 showed high identity to other FHbs …
amino acid sequences of the deduced FHb1 and FHb2 showed high identity to other FHbs …
[HTML][HTML] The X-ray Structure of Ferric Escherichia coliFlavohemoglobin Reveals an Unexpected Geometry of the Distal Heme Pocket
A Ilari, A Bonamore, A Farina, KA Johnson… - Journal of Biological …, 2002 - ASBMB
The x-ray structure of ferric unliganded lipid-free Escherichia coli flavohemoglobin has been
solved to a resolution of 2.2 Å and refined to anR-factor of 19%. The overall fold is similar to …
solved to a resolution of 2.2 Å and refined to anR-factor of 19%. The overall fold is similar to …
A survey of methods for the purification of microbial flavohemoglobins
MES Lewis, HA Corker, B Gollan, RK Poole - Methods in enzymology, 2008 - Elsevier
Over the past decade, the flavohemoglobin Hmp has emerged as the most significant nitric
oxide (NO)–detoxifying protein in many diverse organisms, including yeasts and fungi but …
oxide (NO)–detoxifying protein in many diverse organisms, including yeasts and fungi but …
[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 …