Decarboxylation involving a ferryl, propionate, and a tyrosyl group in a radical relay yields heme b-Reference-Cited by-同舟云学术

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Decarboxylation involving a ferryl, propionate, and a tyrosyl group in a radical relay yields heme b

Published:2018-03 Issue:11 Volume:293 Page:3989-3999
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Streit Bennett R.,Celis Arianna I.,Moraski Garrett C.,Shisler Krista A.,Shepard Eric M.,Rodgers Kenton R.,Lukat-Rodgers Gudrun S.,DuBois Jennifer L.

Funder

HHS National Institutes of Health (NIH)

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference37 articles.

1. Structure and catalytic mechanism of heme oxygenase;Unno;Nat. Prod. Rep,2007

2. Heme oxygenation and the widening paradigm of heme degradation;Wilks;Arch. Biochem. Biophys,2014

3. Heme A synthase does not incorporate molecular oxygen into the formyl group of heme A;Brown;Biochemistry,2004

4. Autocatalytic radical reactions in physiological prosthetic heme modification;Colas;Chem. Rev,2003

5. Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin;Dailey;Proc. Natl. Acad. Sci. U.S.A,2015

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3. Reactivity of Coproheme Decarboxylase with Monovinyl, Monopropionate Deuteroheme;Biomolecules;2023-06-06

4. Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis;Computational and Structural Biotechnology Journal;2023

5. Diverse enzymatic chemistry for propionate side chain cleavages in tetrapyrrole biosynthesis;Journal of Industrial Microbiology and Biotechnology;2023

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