Metalloproteins to Membrane Proteins: Biological Energy Transduction Mechanisms
- Creators
-
Rees, Douglas C.
Abstract
Structural analyses of two macromolecular systems, the metalloprotein nitrogenase and the integral membrane protein MscL (mechanosensitive channel of large conductance), are discussed within the context of energy transduction mechanisms. Nitrogenase catalyzes the ATP dependent reduction of dinitrogen to ammonia during the process of biological nitrogen fixation, while MscL is a stretch activated (mechanosensitive) channel that opens and closes in response to changes in lateral tension applied to membranes. Although nitrogenase and MscL have very different structures and functions, they both mediate the coupling of two energetic processes. From these studies, it is suggested that effective coupling of two processes by transduction proteins occurs through conformational states common to each process.
Additional Information
© 2002 American Chemical Society. Published in print 7 August 2002. I would like to thank the Colonel for his advice and guidance over the years, as well as allowing us to collect the first data sets of the nitrogenase Fe-protein in his lab. None of this work would have been possible without my interactions with Jim Howard, or without the efforts of my group on the projects described from my lab. Research work on nitrogenase and MscL has been supported by NIH grants GM45162 and GM62532, respectively.Additional details
- Eprint ID
- 72588
- Resolver ID
- CaltechAUTHORS:20161206-084656751
- GM45162
- NIH
- GM62532
- NIH
- Created
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2016-12-06Created from EPrint's datestamp field
- Updated
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2021-11-11Created from EPrint's last_modified field
- Series Name
- ACS Symposium Series
- Series Volume or Issue Number
- 827