Spectroscopic characterization of the first ultrafast catalytic intermediate in protochlorophyllide oxidoreductase

O. Sytina; I.H.M. van Stokkum; D.J. Heyes; C.N. Hunter; M.L. Groot

doi:10.1039/c1cp21713e

Spectroscopic characterization of the first ultrafast catalytic intermediate in protochlorophyllide oxidoreductase

O. Sytina, I.H.M. van Stokkum, D.J. Heyes, C.N. Hunter, M.L. Groot

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

The enzyme NADPH:protochlorophyllide oxidoreductase (POR) catalyses the reduction of protochlorophyllide into chlorophyllide, a precursor of chlorophyll a in photosynthetic organisms. The enzyme binds the substrate and the cofactor in the dark and catalysis is initiated by the absorption of light by the substrate. We have carried out spectroscopic measurements with ultrafast time resolution under single pulse conditions, which reveal a biphasic formation of the first catalytic intermediate, I675* with average rates of (3.7 ± 0.7 ps)

Original language	English
Pages (from-to)	616-625
Journal	Physical Chemistry Chemical Physics - PCCP
Volume	14
Issue number	2
DOIs	https://doi.org/10.1039/c1cp21713e
Publication status	Published - 2012

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title = "Spectroscopic characterization of the first ultrafast catalytic intermediate in protochlorophyllide oxidoreductase",

abstract = "The enzyme NADPH:protochlorophyllide oxidoreductase (POR) catalyses the reduction of protochlorophyllide into chlorophyllide, a precursor of chlorophyll a in photosynthetic organisms. The enzyme binds the substrate and the cofactor in the dark and catalysis is initiated by the absorption of light by the substrate. We have carried out spectroscopic measurements with ultrafast time resolution under single pulse conditions, which reveal a biphasic formation of the first catalytic intermediate, I675* with average rates of (3.7 ± 0.7 ps)",

author = "O. Sytina and {van Stokkum}, I.H.M. and D.J. Heyes and C.N. Hunter and M.L. Groot",

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AU - Sytina, O.

AU - van Stokkum, I.H.M.

AU - Heyes, D.J.

AU - Hunter, C.N.

AU - Groot, M.L.

PY - 2012

Y1 - 2012

N2 - The enzyme NADPH:protochlorophyllide oxidoreductase (POR) catalyses the reduction of protochlorophyllide into chlorophyllide, a precursor of chlorophyll a in photosynthetic organisms. The enzyme binds the substrate and the cofactor in the dark and catalysis is initiated by the absorption of light by the substrate. We have carried out spectroscopic measurements with ultrafast time resolution under single pulse conditions, which reveal a biphasic formation of the first catalytic intermediate, I675* with average rates of (3.7 ± 0.7 ps)

AB - The enzyme NADPH:protochlorophyllide oxidoreductase (POR) catalyses the reduction of protochlorophyllide into chlorophyllide, a precursor of chlorophyll a in photosynthetic organisms. The enzyme binds the substrate and the cofactor in the dark and catalysis is initiated by the absorption of light by the substrate. We have carried out spectroscopic measurements with ultrafast time resolution under single pulse conditions, which reveal a biphasic formation of the first catalytic intermediate, I675* with average rates of (3.7 ± 0.7 ps)

U2 - 10.1039/c1cp21713e

DO - 10.1039/c1cp21713e

M3 - Article

SN - 1463-9076

VL - 14

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JO - Physical Chemistry Chemical Physics - PCCP

JF - Physical Chemistry Chemical Physics - PCCP

IS - 2

ER -

Spectroscopic characterization of the first ultrafast catalytic intermediate in protochlorophyllide oxidoreductase

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