The Roles of Thiolate-Heme Proteins, Other Than the P450 Cytochromes, in the Regulation of Heme-Sensor Proteins

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F08%3A10283091" target="_blank" >RIV/00216208:11310/08:10283091 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
The Roles of Thiolate-Heme Proteins, Other Than the P450 Cytochromes, in the Regulation of Heme-Sensor Proteins
Original language description
Cytochrome P450, nitric oxide synthase, and chloroperoxidase are typical thiolate-heme enzymes, in which heme iron coordinated with the cysteine thiolate activates molecular oxygen or hydrogen peroxide. A new group of thiolate-heme proteins is becoming recognized. In these proteins, termed heme-responsive/sensing proteins, or simply heme-sensor proteins, the thiolate-heme iron has a sensor function. All known heme-sensor proteins use a cysteine residue to bind heme. The first question is why cysteine isemployed in this capacity. Ligation of heme with thiolate, the presence of redox-dependent ligand switches, fast heme dissociation rates from the heme-sensor proteins, and formation of 5-coordinated NO-Fe(II) heme complexes, appear to be common characteristics of heme-sensor proteins. The Cys-Pro (CP) motif may also be important for heme binding in some heme-sensor proteins. In this minireview, we summarize the inorganic and physicochemical characters of heme-sensor proteins, and includ
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2008
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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