The first spectroscopic evidence for the binding of a small gaseous molecule to the isolated iron molybdenum cofactor of nitrogenase (FeMoco) is presented: FTIR spectroelectrochemistry in a thin-layer cell shows that reduced FeMoco binds carbon monoxide and gives rise to ν(CO) stretches that are close to those observed during turnover of the enzyme.
S. K. Ibrahim, C. A. Gormal, B. E. Smith, C. J. Pickett, K. Vincent and S. P. Best, Chem. Commun., 1999, 1019 DOI: 10.1039/A902371B
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.
Please wait while we load your content...
