Ultrafast enzymatic reaction dynamics in protochlorophyllide oxidoreductase

Derren J. Heyes; C. Neil Hunter; I. H M Van Stokkum; Rienk Van Grondelle; Marie Louise Groot

doi:10.1038/nsb929

Ultrafast enzymatic reaction dynamics in protochlorophyllide oxidoreductase

Derren J. Heyes, C. Neil Hunter, I. H M Van Stokkum, Rienk Van Grondelle, Marie Louise Groot

Research output: Contribution to journal › Article › peer-review

Abstract

The reaction catalyzed by the light-driven enzyme protochlorophyllide oxidoreductase (POR) has been initiated with a 50-fs laser pulse. We show that the catalytic mechanism, involving proton and hydride transfers, proceeds with time constants of 3 ps and 400 ps. It is known that catalysis by POR involves thermally excited protein dynamics; our results show that these molecular motions occur on an ultrafast timescale.

Original language	English
Pages (from-to)	491-492
Number of pages	1
Journal	Nature Structural Biology
Volume	10
Issue number	6
DOIs	https://doi.org/10.1038/nsb929
Publication status	Published - 1 Jun 2003

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title = "Ultrafast enzymatic reaction dynamics in protochlorophyllide oxidoreductase",

abstract = "The reaction catalyzed by the light-driven enzyme protochlorophyllide oxidoreductase (POR) has been initiated with a 50-fs laser pulse. We show that the catalytic mechanism, involving proton and hydride transfers, proceeds with time constants of 3 ps and 400 ps. It is known that catalysis by POR involves thermally excited protein dynamics; our results show that these molecular motions occur on an ultrafast timescale.",

author = "Heyes, {Derren J.} and Hunter, {C. Neil} and {Van Stokkum}, {I. H M} and {Van Grondelle}, Rienk and Groot, {Marie Louise}",

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AU - Heyes, Derren J.

AU - Hunter, C. Neil

AU - Van Stokkum, I. H M

AU - Van Grondelle, Rienk

AU - Groot, Marie Louise

PY - 2003/6/1

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AB - The reaction catalyzed by the light-driven enzyme protochlorophyllide oxidoreductase (POR) has been initiated with a 50-fs laser pulse. We show that the catalytic mechanism, involving proton and hydride transfers, proceeds with time constants of 3 ps and 400 ps. It is known that catalysis by POR involves thermally excited protein dynamics; our results show that these molecular motions occur on an ultrafast timescale.

U2 - 10.1038/nsb929

DO - 10.1038/nsb929

M3 - Article

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VL - 10

SP - 491

EP - 492

JO - Nature Structural Biology

JF - Nature Structural Biology

IS - 6

ER -

Ultrafast enzymatic reaction dynamics in protochlorophyllide oxidoreductase

Abstract

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