Results 251 to 260 of about 207,281 (307)

Electrochemistry of immobilized hemes and heme proteins

, 2007
openaire   +1 more source

Environmental Heme Utilization by Heme-Auxotrophic Bacteria

, 2012
Heme, an iron-containing porphyrin, is the prosthetic group for numerous key cellular enzymatic and regulatory processes. Many bacteria encode the biosynthetic enzymes needed for autonomous heme production. Remarkably, however, numerous other bacteria lack a complete heme biosynthesis pathway, yet encode heme-requiring functions.
Gruss, Alexandra, Borezée-Durant, Elise, Lechardeur, Delphine   +2 more
openaire   +5 more sources

Multiheme proteins: effect of heme–heme interactions

Dalton Transactions, 2018
This Frontier illustrates a brief personal account on the effect of heme–heme interactions in dihemes which thereby discloses some of the evolutionary design principles involved in multiheme proteins for their diverse structures and functions.
Dipti Lai, Firoz Shah Tuglak Khan, Sankar Prasad Rath   +2 more
openaire   +3 more sources

The Diversity of Heme Sensor Systems - Heme-Responsive Transcriptional Regulation Mediated by Transient Heme Protein Interactions.

FEMS Microbiology Reviews, 2022
Heme is a versatile molecule that is vital for nearly all cellular life by serving as prosthetic group for various enzymes or as nutritional iron source for diverse microbial species. However, elevated levels of heme is toxic to cells.
Julia Frunzke, Aileen Krüger, Marc Keppel   +2 more
exaly   +2 more sources

Some of the next articles are maybe not open access.

Related searches:

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, Tadashi, Yoshida, Masato, Noguchi   +2 more
openaire   +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
openaire   +2 more sources

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
openaire   +2 more sources