A structural model for the nucleotide binding domains of the flavocytochrome b–245 β‐chain
NADPH is a system in phagocytic cells that generates O2− and hydrogen peroxide in the
endocytic vacuole, both of which are important for killing of the engulfed microbe …
endocytic vacuole, both of which are important for killing of the engulfed microbe …
[HTML][HTML] Nature of the FeO2 bonding in myoglobin and hemoglobin: A new molecular paradigm
K Shikama - Progress in biophysics and molecular biology, 2006 - Elsevier
The iron (II)–dioxygen bond in myoglobin and hemoglobin is a subject of wide interest.
Studies range from examinations of physical–chemical properties dependent on its …
Studies range from examinations of physical–chemical properties dependent on its …
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 …
The simplest contain protohaem as sole prosthetic group, but show considerable variation in …
The process of hypoxic induction of Daphnia magna hemoglobin: subunit composition and functional properties
B Zeis, B Becher, T Lamkemeyer, S Rolf… - … and Physiology Part B …, 2003 - Elsevier
The process of oxygen-dependent hemoglobin induction in Daphnia magna was studied
over an 11-day period of hypoxia (ambient oxygen partial pressure: 3 kPa). Along with the …
over an 11-day period of hypoxia (ambient oxygen partial pressure: 3 kPa). Along with the …
Lucina pectinata oxyhemoglobin (II-III) heterodimer pH susceptibility
D Marchany-Rivera, CA Smith… - Journal of inorganic …, 2020 - Elsevier
Lucina pectinata live in high concentrations of hydrogen sulfide (H 2 S) and contains one
hemoglobin, Hemoglobin I (HbI), transporting H 2 S and two hemoglobins, Hemoglobin II …
hemoglobin, Hemoglobin I (HbI), transporting H 2 S and two hemoglobins, Hemoglobin II …
Escherichia coli flavohaemoglobin (Hmp) reduces cytochrome c and Fe(III)-hydroxamate K by electron transfer from NADH via FAD: sensitivity of oxidoreductase …
RK Poole, NJ Rogers, RAM D'mello… - …, 1997 - microbiologyresearch.org
Escherichia coli flavohaemoglobin (Hmp) reduced purified mitochondrial cytochrome c
aerobically in a reaction that was not substantially inhibited by superoxide dismutase …
aerobically in a reaction that was not substantially inhibited by superoxide dismutase …
H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin
FP Nicoletti, E Droghetti, BD Howes… - … et Biophysica Acta (BBA …, 2013 - Elsevier
The ferric form of truncated hemoglobin II from Thermobifida fusca (Tf-trHb) and its triple
mutant WG8F-YB10F-YCD1F at neutral and alkaline pH, and in the presence of CN− have …
mutant WG8F-YB10F-YCD1F at neutral and alkaline pH, and in the presence of CN− have …
Crystallization and preliminary X‐ray diffraction studies of a bacterial flavohemoglobin protein
U Ermler, RA Siddiqui, R Cramm… - Proteins: Structure …, 1995 - Wiley Online Library
A flavohemoglobin protein (FHP) was isolated from Alcaligenes eutrophus and has been
crystallized by vapor diffusion methods using PEG 3350 as precipitant. The crystals of the …
crystallized by vapor diffusion methods using PEG 3350 as precipitant. The crystals of the …
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 …
of several alkylhydroperoxide substrates into their corresponding alcohols using NADH as …