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PhuS conformational dynamics are essential for DNA binding and heme-responsive control of the prrF operon in Pseudomonas aeruginosa. [PDF]

J Biol Chem
Egoshi R, Huang W, Albert T, Kane MA, Deredge D, Moënne-Loccoz P, Wilks A.   +6 more
europepmc   +1 more source

Electrochemistry of immobilized hemes and heme proteins

, 2007
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Heme oxygenase and heme degradation

Biochemical and Biophysical Research Communications, 2005
The microsomal heme oxygenase system consists of heme oxygenase (HO) and NADPH-cytochrome P450 reductase, and plays a key role in the physiological catabolism of heme which yields biliverdin, carbon monoxide, and iron as the final products. Heme degradation proceeds essentially as a series of autocatalytic oxidation reactions involving heme bound to HO.
Goro Kikuchi
exaly   +3 more sources

THE HEME OXYGENASE SYSTEM:A Regulator of Second Messenger Gases

Annual Review of Pharmacology and Toxicology, 1997
Mahin D Maines, M D Maines
exaly   +2 more sources

Protonated Heme

Chemistry – A European Journal, 2007
AbstractThe ions formally corresponding to protonated heme [FeII–hemeH]+ have been obtained by collision‐induced dissociation from the electrospray ionization of microperoxidase (MP11) and their gas‐phase chemistry has been studied by FTICR mass spectrometry.
CHIAVARINO, Barbara, CRESTONI, Maria Elisa, FORNARINI, Simonetta, Carme Rovira   +3 more
openaire   +3 more sources

Evidence of heme-heme interaction in heme-spin-labeled hemoglobin

Biochemical and Biophysical Research Communications, 1971
Summary Two kinds of valency hybrid hemoglobins containing spin-labeled ferric heme in one type of subunit were prepared. The electron paramagnetic resonance spectra of the α-(αSLFe +++ -βFe ++ O 2 ) and 3-(α-Fe ++ O 2 -βSLFe +++ ) spin-labeled hemoglobins were different, suggesting their non-equivalent conformational properties in hemoglobin ...
T, Asakura, H R, Drott
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Heme biosynthesis in prokaryotes.

Biochimica et biophysica acta. Molecular cell research, 2020
The cyclic tetrapyrrole heme is used as a prosthetic group in a broad variety of different proteins in almost all organisms. Often, it is essential for vital biochemical processes such as aerobic and anaerobic respiration as well as photosynthesis.
G. Layer
semanticscholar   +1 more source

Mechanism of heme degradation by heme oxygenase

Journal of Inorganic Biochemistry, 2000
Heme oxygenase catalyzes the three step-wise oxidation of hemin to alpha-biliverdin, via alpha-meso-hydroxyhemin, verdoheme, and ferric iron-biliverdin complex. This enzyme is a simple protein which does not have any prosthetic groups. However, heme and its two metabolites, alpha-meso-hydroxyhemin and verdoheme, combine with the enzyme and activate ...
T, Yoshida, C T, Migita
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Heme-heme interaction in cytochrome oxidase

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1972
Abstract The cytochromes a and a 3 of intact pigeon heart mitochondria are shown to contribute equally to the α band of cytochrome oxidase in the absence of added ligands. The oxidation-reduction midpoint potentials of the cytochromes a and a 3 at pH 7·2 are −220 mV and +380 mV, respectively.
D F, Wilson, J G, Lindsay, E S, Brocklehurst   +2 more
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