Structural domains of P450-containing monooxygenase systems |
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| Authors: | Degtyarenko Kirill N |
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| Affiliation: | International Centre for Genetic Engineering and Biotechnology, Area Science Park 34012 Trieste, Italy and Institute of Biomedical Chemistry, Pogodinskaya 10, 119832 Moscow, Russia Present address: Department of Biochemistry and Molecular Biology, University of Leeds, Leeds LS2 9JT, UK. |
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| Abstract: | All known P450-containing monooxygenase systems share commonstructural and functional domain architecture. Apart from P450itself, these systems can comprise several fundamentally differentprotein components or domains, all of which are shared by othermulticomponent/multidomain enzyme systems with various functions:FAD flavoprotein or domain, FMN domain, Fe2S2 ferredoxin, Fe3S4ferredoxin, and cytochrome b5. Either FMN domain, ferredoxinsor cytochrome bs serve as the electron transport intermediatebetween the FAD domain and P450. The molecular evolution ofboth P450-containing systems and of each particular componentdoes not follow phylogeny in general. Gene fusion and horizontalgene transfer events can lead to the appearance of novel redoxchains in the same manner that artificial chimeric proteinscan be constructed by humans. Recent studies using genetic andprotein engineering techniques to investigate the separate domainsand their interaction are described. |
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| Keywords: | cytochrome b5/ ferredoxin:NADP+ reductase/ flavodoxin/ iron-sulphur proteins/ nitric oxide synthase/ nitric oxide reductase/ P450-containing monooxygenase systems/ redox domains |
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