The Escherichia coli Periplasmic Aldehyde Oxidoreductase Is an Exceptional Member of the Xanthine Oxidase Family of Molybdoenzymes-Reference-Cited by-同舟云学术

The Escherichia coli Periplasmic Aldehyde Oxidoreductase Is an Exceptional Member of the Xanthine Oxidase Family of Molybdoenzymes

Published:2016-09-13 Issue:10 Volume:11 Page:2923-2935
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

Correia Márcia A. S.¹,Otrelo-Cardoso Ana Rita¹,Schwuchow Viola²,Sigfridsson Clauss Kajsa G. V.³,Haumann Michael³,Romão Maria João¹,Leimkühler Silke²,Santos-Silva Teresa¹

Affiliation:

1. UCIBIO/Requimte, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal

2. Institut für Biologie und Biochemie, Universität Potsdam, Am Neuen Palais 10, 14469 Potsdam, Deutschland

3. Freie Universität Berlin, Fachbereich Physik, 14195 Berlin, Germany

Funder

Deutsche Forschungsgemeinschaft

Wenner-Gren Foundation

Fundação para a Ciência e a Tecnologia

Stiftelsen Bengt Lundqvist minne

European Regional Development Fund

Publisher

American Chemical Society (ACS)

Subject

Molecular Medicine,General Medicine,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acschembio.6b00572

Reference50 articles.

1. Molybdenum Nitrogenases

2. The pterin molybdenum cofactors.

3. Molybdenum and tungsten enzymes: a crystallographic and mechanistic overview

4. Molybdopterin adenine dinucleotide and molybdopterin hypoxanthine dinucleotide in formylmethanofuran dehydrogenase fromMethanobacterium thermoautotrophicum(Marburg)

5. Molybdenum cofactor biosynthesis in Escherichia coli. Requirement of the chlB gene product for the formation of molybdopterin guanine dinucleotide

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