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Femtosecond dynamics of flavoproteins: Charge separation and recombination in riboflavine (vitamin B_2)-binding protein and in glucose oxidase enzyme

Zhong, Dongping and Zewail, Ahmed H. (2001) Femtosecond dynamics of flavoproteins: Charge separation and recombination in riboflavine (vitamin B_2)-binding protein and in glucose oxidase enzyme. Proceedings of the National Academy of Sciences of the United States of America, 98 (21). pp. 11867-11872. ISSN 0027-8424. PMCID PMC59734. https://resolver.caltech.edu/CaltechAUTHORS:ZHOpnas01a

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Abstract

Flavoproteins can function as hydrophobic sites for vitamin B_2 (riboflavin) or, in other structures, with cofactors for catalytic reactions such as glucose oxidation. In this contribution, we report direct observation of charge separation and recombination in two flavoproteins: riboflavin-binding protein and glucose oxidase. With femtosecond resolution, we observed the ultrafast electron transfer from tryptophan(s) to riboflavin in the riboflavin-binding protein, with two reaction times: approx 100 fs (86% component) and 700 fs (14%). The charge recombination was observed to take place in 8 ps, as probed by the decay of the charge-separated state and the recovery of the ground state. The time scale for charge separation and recombination indicates the local structural tightness for the dynamics to occur that fast and with efficiency of more than 99%. In contrast, in glucose oxidase, electron transfer between flavin-adenine-dinucleotide and tryptophan(s)/tyrosine(s) takes much longer times, 1.8 ps (75%) and 10 ps (25%); the corresponding charge recombination occurs on two time scales, 30 ps and nanoseconds, and the efficiency is still more than 97%. The contrast in time scales for the two structurally different proteins (of the same family) correlates with the distinction in function: hydrophobic recognition of the vitamin in the former requires a tightly bound structure (ultrafast dynamics), and oxidation-reduction reactions in the latter prefer the formation of a charge-separated state that lives long enough for chemistry to occur efficiently. Finally, we also studied the influence on the dynamics of protein conformations at different ionic strengths and denaturant concentrations and observed the sharp collapse of the hydrophobic cleft and, in contrast, the gradual change of glucose oxidase.


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http://www.pnas.org/content/98/21/11867.longPublisherArticle
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC59734/PubMed CentralArticle
Additional Information:© 2001, The National Academy of Sciences. Contributed by Ahmed H. Zewail, August 20, 2001. We thank Prof. Hugo L. Monaco (University of Verona, Italy) for providing the RF-binding protein coordinates. Special thanks also to Drs. Chaozhi Wan and Samir Pal for their discussion and help. This work was supported by the National Science Foundation. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. §1734 solely to indicate this fact.
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Subject Keywords:riboflavin, flavin-adenine-dinucleotide RfBP, riboflavin-binding protein, glucose oxidase, electron transfer, guanidine hydrochloride
Issue or Number:21
PubMed Central ID:PMC59734
Record Number:CaltechAUTHORS:ZHOpnas01a
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:ZHOpnas01a
Alternative URL:http://www.pnas.org/cgi/content/abstract/98/21/11867
Official Citation:Dongping Zhong and Ahmed H. Zewail Femtosecond dynamics of flavoproteins: Charge separation and recombination in riboflavine (vitamin B2)-binding protein and in glucose oxidase enzyme PNAS 2001 98 (21) 11867-11872; doi:10.1073/pnas.211440398
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:506
Collection:CaltechAUTHORS
Deposited By: Archive Administrator
Deposited On:11 Jul 2005
Last Modified:02 Oct 2019 22:34

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