Issue 6, 2012
From the journal:

Chemical Communications

Spectroscopic characterization of the key catalytic intermediate Ni–C in the O2-tolerant [NiFe] hydrogenase I from Aquifex aeolicus: evidence of a weakly bound hydride†‡

Maria-Eirini Pandelia,a   Pascale Infossi,b   Matthias Stein,c   Marie-Thérèse Giudici-Orticonib  and  Wolfgang Lubitz*a  

* Corresponding authors

a Max-Planck-Institut für Bioanorganische Chemie, Stiftstr. 34-36, 45470 M, Germany
E-mail: wolfgang.lubitz@mpi-mail.mpg.de

b Laboratoire de Bioénergétique et Ingénierie des Protéines, IMM-CNRS, Marseille, France
E-mail: giudici@ifr88.cnrs-mrs.fr

c Max-Planck-Institut für Dynamik komplexer technischer Systeme, Sandtorstr. 1, 39106 Magdeburg, Germany
E-mail: matthias.stein@mpi-magdeburg.mpg.de

Abstract

Ni–C in the O2-tolerant hydrogenase I from Aquifex aeolicus binds a hydride weaker than that in O2-sensitive hydrogenases. This is in line with the enhanced light-sensitivity of Ni–C, greater lability of the hydride complex and increased catalytic redox potentials relevant to bio-H2 oxidation.

Graphical abstract: Spectroscopic characterization of the key catalytic intermediate Ni–C in the O2-tolerant [NiFe] hydrogenase I from Aquifex aeolicus: evidence of a weakly bound hydride

About
Cited by
Related
Download options Please wait...

Supplementary files

Article information

DOI
https://doi.org/10.1039/C1CC16109A
Article type
Communication
Submitted
30 Sep 2011
Accepted
14 Nov 2011
First published
05 Dec 2011

Chem. Commun., 2012,48, 823-825

Permissions

Request permissions

Spectroscopic characterization of the key catalytic intermediate Ni–C in the O2-tolerant [NiFe] hydrogenase I from Aquifex aeolicus: evidence of a weakly bound hydride

M. Pandelia, P. Infossi, M. Stein, M. Giudici-Orticoni and W. Lubitz, Chem. Commun., 2012, 48, 823 DOI: 10.1039/C1CC16109A

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements