TY - GEN
T1 - Contribution of time-resolved absorption spectroscopy to study biological questions
AU - Yoo, Byung Kuk
AU - Lamarre, Isabelle
AU - Martin, Jean Louis
AU - Negrerie, Michel
N1 - Publisher Copyright:
© Springer-Verlag Berlin Heidelberg 2011.
PY - 2011/1/1
Y1 - 2011/1/1
N2 - In this report, we illustrate through the study of two allosteric heme proteins the contribution of time-resolved absorption spectroscopy to the understanding of fundamental biological mechanisms. The first studied protein is the endogenous nitric oxide receptor (guanylate cyclase, sGC) whose activation and deactivation mechanisms are not yet fully resolved. We show that the rebinding of the proximal histidine occurs in ~100 picoseconds in sGC, which is the very first step of its deactivation following NO release. We also show that synergistic action of CO together with an allosteric activator induces the cleavage of the bond between heme iron and proximal histidine. The second one is the prototype of allosteric protein, the dioxygen transporter hemoglobin (Hb). In Hb, we show that the motion of the iron atom, central to the heme, moves in ~18 picoseconds after NO binding; this motion represents the very first step of the allosteric T → R transition.
AB - In this report, we illustrate through the study of two allosteric heme proteins the contribution of time-resolved absorption spectroscopy to the understanding of fundamental biological mechanisms. The first studied protein is the endogenous nitric oxide receptor (guanylate cyclase, sGC) whose activation and deactivation mechanisms are not yet fully resolved. We show that the rebinding of the proximal histidine occurs in ~100 picoseconds in sGC, which is the very first step of its deactivation following NO release. We also show that synergistic action of CO together with an allosteric activator induces the cleavage of the bond between heme iron and proximal histidine. The second one is the prototype of allosteric protein, the dioxygen transporter hemoglobin (Hb). In Hb, we show that the motion of the iron atom, central to the heme, moves in ~18 picoseconds after NO binding; this motion represents the very first step of the allosteric T → R transition.
U2 - 10.1007/978-3-642-17913-6_15
DO - 10.1007/978-3-642-17913-6_15
M3 - Conference contribution
AN - SCOPUS:85032967312
SN - 9783642179129
T3 - Springer Proceedings in Physics
SP - 123
EP - 134
BT - EKC 2010 - Proceedings of the EU-Korea Conference on Science and Technology
A2 - Lee, Jehyun
A2 - Han, Man-Wook
PB - Springer Science and Business Media, LLC
T2 - 3rd EU Korea Conference on Science and Technology, EKC 2010
Y2 - 29 July 2010 through 31 July 2010
ER -