R
Rita Bernhardt
Researcher at Saarland University
Publications - 263
Citations - 9200
Rita Bernhardt is an academic researcher from Saarland University. The author has contributed to research in topics: Adrenodoxin & Adrenodoxin reductase. The author has an hindex of 45, co-authored 260 publications receiving 8200 citations.
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Cytochromes P450 as versatile biocatalysts.
TL;DR: The set of interesting reactions being catalysed by cytochromes P450 systems and the availability of new genetic engineering techniques allowing to heterologously express them and to improve and change their activity, stability and selectivity makes them promising candidates for biotechnological application in the future.
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Cytochrome P450 systems--biological variations of electron transport chains.
TL;DR: The classical as well as the recently discovered P450 redox systems are compiled in this paper and classified according to their composition.
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Cytochromes P450 as promising catalysts for biotechnological application: chances and limitations.
Rita Bernhardt,Vlada B. Urlacher +1 more
TL;DR: A critical overview about possibilities and chances for application of these interesting catalysts as well as to discuss drawbacks and problems related to their use are given.
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Humans possess two mitochondrial ferredoxins, Fdx1 and Fdx2, with distinct roles in steroidogenesis, heme, and Fe/S cluster biosynthesis.
Alex D. Sheftel,Oliver Stehling,Antonio J. Pierik,Hans-Peter Elsässer,Ulrich Mühlenhoff,Holger Webert,Anna Hobler,Frank Hannemann,Rita Bernhardt,Roland Lill +9 more
TL;DR: It is concluded that mammals depend on two distinct mitochondrial ferredoxins for the specific production of either steroid hormones or heme A and Fe/S proteins.
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Adrenodoxin: Structure, stability, and electron transfer properties
TL;DR: The recently solved first crystal structure of the vertebrate‐type ferredoxin, the truncated adrenodoxin Adx(4‐108), is discussed, that offers the unique opportunity for better understanding of the structure‐function relationships and stabilization of this protein, as well as of the molecular architecture of [2Fe‐2S] ferredoxins in general.