Bacterial (CYP101) and mitochondrial P450 systems-how comparable are they?

No abstract is available for this paper.

• Publication year

  2003

• Venue

  Biochemical and Biophysical Research Communications - BBRC

• Publication date

  2003-12-05

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/J.BBRC.2003.09.214PMID 14630046
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• A conserved histidine in vertebrate-type ferredoxins is critical for redox-dependent dynamics.

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  2002cited by this paper
• Comparison of functional domains in vertebrate-type ferredoxins.

  2002cited by this paper
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• The Interaction of Bovine Adrenodoxin with CYP11A1 (Cytochrome P450scc) and CYP11B1 (Cytochrome P45011β)

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• Modelling of three-dimensional structures of cytochromes P450 11B1 and 11B2.

  2001cited by this paper
• Crystal structures of adrenodoxin reductase in complex with NADP+ and NADPH suggesting a mechanism for the electron transfer of an enzyme family.

  2000cited by this paper
• The catalytic pathway of cytochrome p450cam at atomic resolution.

  2000cited by this paper
• Molecular modeling of mammalian cytochromes P450: application to study enzyme function.

  2000cited by this paper
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  2000cited by this paper
• Putidaredoxin-Cytochrome P450cam Interaction

  1999cited by this paper
• The structure of adrenodoxin reductase of mitochondrial P450 systems: electron transfer for steroid biosynthesis.

  1999cited by this paper
• Binding and Electron Transfer between Putidaredoxin and Cytochrome P450cam. Theory and Experiments

  1998cited by this paper
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  1998cited by this paper
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  1997cited by this paper
• Molecular recognition and electron transfer in mitochondrial steroid hydroxylase systems.

  1997cited by this paper
• Specific Aspects of Electron Transfer from Adrenodoxin to Cytochromes P450scc and P45011β*

  1997cited by this paper
• Probing the Interactions of Putidaredoxin with Redox Partners in Camphor P450 5-Monooxygenase by Mutagenesis of Surface Residues*

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• A structure-based model for cytochrome P450cam-putidaredoxin interactions.

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  1995cited by this paper
• Mutational effects on the spectroscopic properties and biological activities of oxidized bovine adrenodoxin, and their structural implications.

  1995cited by this paper
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  1994cited by this paper
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  1994cited by this paper
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  1992cited by this paper
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  1992cited by this paper
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  1981cited by this paper
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  1979cited by this paper
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  1979cited by this paper
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  1978cited by this paper
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  1974cited by this paper
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