Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 112, Issue 45, Pages 13845-13849Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1519696112
Keywords
nitrogenase; vanadium; carbon monoxide; turnover; substrate binding
Categories
Funding
- NIH [R01 GM67626, P41GM103393]
- Department of Energy (DOE) Basic Energy Sciences
- NIH National Institute of General Medical Sciences [P41GM103393]
- DOE Basic Environmental Research
Ask authors/readers for more resources
Biocatalysis by nitrogenase, particularly the reduction of N-2 and CO by this enzyme, has tremendous significance in environmentand energy-related areas. Elucidation of the detailed mechanism of nitrogenase has been hampered by the inability to trap substrates or intermediates in a well-defined state. Here, we report the capture of substrate CO on the resting-state vanadium-nitrogenase in a catalytically competent conformation. The close resemblance of this active CO-bound conformation to the recently described structure of CO-inhibited molybdenum-nitrogenase points to the mechanistic relevance of sulfur displacement to the activation of iron sites in the cofactor for CO binding. Moreover, the ability of vanadium-nitrogenase to bind substrate in the resting-state uncouples substrate binding from subsequent turnover, providing a platform for generation of defined intermediate(s) of both CO and N-2 reduction.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available