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Cytochrome P450 systems--biological variations of electron transport chains.
Humans possess two mitochondrial ferredoxins, Fdx1 and Fdx2, with distinct roles in steroidogenesis, heme, and Fe/S cluster biosynthesis
- A. Sheftel, O. Stehling, R. Lill
- Biology, ChemistryProceedings of the National Academy of Sciences
- 14 June 2010
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.
Adrenodoxin: Structure, stability, and electron transfer properties
- A. Grinberg, F. Hannemann, Burkhard Schiffler, Jürgen J. Müller, U. Heinemann, R. Bernhardt
- Biology, ChemistryProteins
- 1 September 2000
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.
Human aldosterone synthase: Recombinant expression in E. coli and purification enables a detailed biochemical analysis of the protein on the molecular level
A new cytochrome P450 system from Bacillus megaterium DSM319 for the hydroxylation of 11-keto-β-boswellic acid (KBA)
- E. Brill, F. Hannemann, J. Zapp, Gerit Brüning, J. Jauch, R. Bernhardt
- BiologyApplied Microbiology and Biotechnology
- 1 February 2014
The CYP106A1 system was able to convert the pentacyclic triterpene 11-keto-β-boswellic acid (KBA) belonging to the main bioactive constituents of Boswellia serrata gum resin extracts, which are used to treat inflammatory disorders and arthritic diseases.
Efficient conversion of 11-deoxycortisol to cortisol (hydrocortisone) by recombinant fission yeast Schizosaccharomyces pombe.
The adrenodoxin-like ferredoxin of Schizosaccharomyces pombe mitochondria.
CYP105A1 mediated 3-hydroxylation of glimepiride and glibenclamide using a recombinant Bacillus megaterium whole-cell catalyst.
The CYP11B subfamily
A new Bacillus megaterium whole-cell catalyst for the hydroxylation of the pentacyclic triterpene 11-keto-β-boswellic acid (KBA) based on a recombinant cytochrome P450 system
- S. Bleif, F. Hannemann, J. Zapp, D. Hartmann, J. Jauch, R. Bernhardt
- Biology, ChemistryApplied Microbiology and Biotechnology
- 1 February 2012
This work developed for the first time an expression system for cytochromes P450 in B. megaterium for the uptake of acids with terpene structure and revealed a 15α-hydroxylation of the anti-inflammatory pentacyclic triterpene 11-Keto-β-boswellic acid.