The Non-Heme Diiron Alkane Monooxygenase of Pseudomonas oleovorans (AlkB) Hydroxylates via a Substrate Radical Intermediate-Reference-Cited by-同舟云学术

The Non-Heme Diiron Alkane Monooxygenase of Pseudomonas oleovorans (AlkB) Hydroxylates via a Substrate Radical Intermediate

Published:2000-11-01 Issue:47 Volume:122 Page:11747-11748
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Austin Rachel N.¹,Chang Hung-Kuang¹,Zylstra Gerben J.¹,Groves John T.¹

Affiliation:

1. Department of Chemistry, Princeton University Princeton, New Jersey 08544 Biotechnology Center for Agriculture and the Environment Rutgers University, New Brunswick New Jersey 08901

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja001500v

Reference31 articles.

1. Recent 16S rRNA sequencing by van Beilen and Witholt has reclassifiedPseudomonas oleovoransTF4-1L asP. putida(GenBank accession AJ249825). To facilitate further communication, we have elected to use the older name and acknowledge the nomenclature issue here.

2. Enzymatic ω-Oxidation

3. Production of primary aliphatic alcohols with a recombinant Pseudomonas strain, encoding the alkane hydroxylase enzyme system

4. Developments toward large-scale bacterial bioprocesses in the presence of bulk amounts of organic solvents

5. Mossbauer studies of alkane -hydroxylase: Evidence for a diiron cluster in an integral-membrane enzyme

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