Publication:

Examining reactivity and specificity of cytochrome c peroxidase by using combinatorial mutagenesis

cris.lastimport.scopus

2024-08-07T11:39:20Z

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81348

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LIP

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ISIC

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SB

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EPFL

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F-1726-2015

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Johnsson, Kai

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datacite.rights

metadata-only

dc.contributor.author

Wilming, Martin

dc.contributor.author

Iffland, Andre

dc.contributor.author

Tafelmeyer, Petra

dc.contributor.author

Arrivoli, Claudio

dc.contributor.author

Saudan, Christophe

dc.contributor.author

Johnsson, Kai

dc.date.accessioned

2006-02-27T13:53:06

dc.date.available

2006-02-27T13:53:06

dc.date.created

2006-02-27

dc.date.issued

2002

dc.date.modified

2025-01-24T04:05:04.672591Z

dc.description.abstract

Combinatorial mutagenesis was used to investigate the role of three key residues in cytochrome c peroxidase (CCP) from Saccharomyces cerevisiae, Arg48, Trp51, and Trp191, in control of the reactivity and selectivity of the heme-contg. enzyme. Libraries were prepd. by randomization of these residues and were subsequently screened for activity against the phenolic substrate guaiacol. Screening conditions were employed that favor either mutants with high activity or those with both high activity and stability of the reactive enzyme intermediates. The results obtained suggest a dual role for Arg48 of CCP; in addn. to stabilizing reactive enzyme intermediates, the distal arginine residue plays a major role in restriction of access to the ferryl oxygen atom by small mols. and thereby controls reactivity and substrate specificity of the peroxidase. At position 51 of CCP, either a phenylalanine or a tryptophan residue is required both for catalytic and structural reasons. In contrast, either polar or pos. charged residues are accepted at the position of Trp191, which is located inside the core of the protein. The variability at position 191 can be interpreted as a reflection of the mechanism of cytochrome c peroxidase, which transforms the nonpolar Trp191 into a transient cation radical. [on SciFinder (R)]

dc.description.sponsorship

LIP

dc.identifier.dar

1046

dc.identifier.doi

10.1002/1439-7633(20021104)3:11<1097::AID-CBIC1097>3.0.CO;2-4

dc.identifier.isi

WOS:000179111600008

dc.identifier.uri

https://infoscience.epfl.ch/handle/20.500.14299/226636

dc.relation.journal

ChemBioChem

dc.title

Examining reactivity and specificity of cytochrome c peroxidase by using combinatorial mutagenesis

dc.type

text::journal::journal article::research article

dspace.entity.type

Publication

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oai:infoscience.tind.io:81348

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Journal Articles

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ARTICLE

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SB

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OpenAIREv4

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article

epfl.peerreviewed

REVIEWED

epfl.publication.version

http://purl.org/coar/version/c_970fb48d4fbd8a85

epfl.writtenAt

EPFL

oaire.citation.endPage

1104

oaire.citation.issue

11

oaire.citation.startPage

1097

oaire.citation.volume

3

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