Journal
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
Volume 5, Issue 5, Pages 804-808Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jz4027425
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Funding
- Institute for Basic Science (IBS) [CA1401-01]
- National Institutes of Health (NIH) National Institute of General Medical Sciences [P41GM103543]
- U.S. Department of Energy, Basic Energy Sciences, Office of Science [DE-AC02-06CH11357]
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Conformational substates of proteins are generally considered to play important roles in regulating protein functions, but an understanding of how they influence the structural dynamics and functions of the proteins has been elusive. Here, we investigate the structural dynamics of sperm whale myoglobin associated with the conformational substates using picosecond X-ray solution scattering. By applying kinetic analysis considering all of the plausible candidate models, we establish a kinetic model for the entire cycle of the protein transition in a wide time range from 100 ps to 10 ms. Four structurally distinct intermediates are formed during the cycle, and most importantly, the transition from the first intermediate to the second one (B -> C) occurs biphasically. We attribute the biphasic kinetics to the involvement of two conformational substates of the first intermediate, which are generated by the interplay between the distal histidine and the photodissociated CO.
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