Properties of the high‐spin heme of MauG are altered by binding of preMADH at the protein surface 40 Å away-Reference-Cited by-同舟云学术

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Properties of the high‐spin heme of MauG are altered by binding of preMADH at the protein surface 40 Å away

Published:2017-05-23 Issue:11 Volume:591 Page:1566-1572
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:FEBS Lett

Author:

Feng Manliang¹,Ma Zhongxin²,Crudup Breland F.¹,Davidson Victor L.²^ORCID

Affiliation:

1. Department of Chemistry Tougaloo College MS USA

2. Burnett School of Biomedical Sciences College of Medicine University of Central Florida Orlando FL USA

Funder

National Institute of General Medical Sciences

National Institutes of Health

National Science Foundation

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/1873-3468.12666

Reference37 articles.

1. MauG, a Novel Diheme Protein Required for Tryptophan Tryptophylquinone Biogenesis

2. Posttranslational Biosynthesis of the Protein-Derived Cofactor Tryptophan Tryptophylquinone

3. Further Insights into Quinone Cofactor Biogenesis: Probing the Role of mauG in Methylamine Dehydrogenase Tryptophan Tryptophylquinone Formation

4. Pyrroloquinoline quinone (PQQ) from methanol dehydrogenase and tryptophan tryptophylquinone (TTQ) from methylamine dehydrogenase

5. A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical

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