The Hydroxide Complex of Pseudomonas aeruginosa Heme Oxygenase as a Model of the Low-Spin Iron(III) Hydroperoxide Intermediate in Heme Catabolism: 13C NMR Spectroscopic Studies Suggest the Active Participation of the Heme in Macrocycle Hydroxylation-Reference-Cited by-同舟云学术

The Hydroxide Complex of Pseudomonas aeruginosa Heme Oxygenase as a Model of the Low-Spin Iron(III) Hydroperoxide Intermediate in Heme Catabolism: 13C NMR Spectroscopic Studies Suggest the Active Participation of the Heme in Macrocycle Hydroxylation

Published:2003-09-04 Issue:39 Volume:125 Page:11842-11852
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Caignan Gregori A.¹,Deshmukh Rahul¹,Zeng Yuhong¹,Wilks Angela¹,Bunce Richard A.¹,Rivera Mario¹

Affiliation:

1. Contribution from the Department of Chemistry, The University of Kansas, Lawrence, Kansas 66045-7582, Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, Maryland 21201-1180, and Department of Chemistry, Oklahoma State University, Stillwater, Oklahoma 74078

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja036147i

Reference42 articles.

1. Microsomal Heme Oxygenase

2. Oxygenated form of heme . heme oxygenase complex and requirement for second electron to initiate heme degradation from the oxygenated complex.

3. Heme oxygenase (HO-1). Evidence for electrophilic oxygen addition to the porphyrin ring in the formation of alpha-meso-hydroxyheme.

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