An S-Oxygenated [NiFe] Complex Modelling Sulfenate Intermediates of an O2-Tolerant Hydrogenase

Nils J. Lindenmaier; Stefan Wahlefeld; Eckhard Bill; Tibor Szilvási; Christopher Eberle; Shenglai Yao; Peter Hildebrandt; Marius Horch; Ingo Zebger; Matthias Driess

doi:10.1002/anie.201611069

An S-Oxygenated [NiFe] Complex Modelling Sulfenate Intermediates of an O₂-Tolerant Hydrogenase

Nils J. Lindenmaier, Stefan Wahlefeld, Eckhard Bill, Tibor Szilvási, Christopher Eberle, Shenglai Yao, Peter Hildebrandt, Marius Horch^*, Ingo Zebger, Matthias Driess

^*Corresponding author for this work

Chemistry

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

Abstract

To understand the molecular details of O₂-tolerant hydrogen cycling by a soluble NAD⁺-reducing [NiFe] hydrogenase, we herein present the first bioinspired heterobimetallic S-oxygenated [NiFe] complex as a structural and vibrational spectroscopic model for the oxygen-inhibited [NiFe] active site. This compound and its non-S-oxygenated congener were fully characterized, and their electronic structures were elucidated in a combined experimental and theoretical study with emphasis on the bridging sulfenato moiety. Based on the vibrational spectroscopic properties of these complexes, we also propose novel strategies for exploring S-oxygenated intermediates in hydrogenases and similar enzymes.

Original language	English
Pages (from-to)	2208-2211
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	56
Issue number	8
DOIs	https://doi.org/10.1002/anie.201611069
Publication status	Published - 1 Jan 2017

Keywords

enzyme models
IR spectroscopy
resonance Raman spectroscopy
spectroscopic models
[NiFe] hydrogenases

Access to Document

10.1002/anie.201611069

Cite this

@article{45a264634d6c43c78c9a433d502dfd41,

title = "An S-Oxygenated [NiFe] Complex Modelling Sulfenate Intermediates of an O2-Tolerant Hydrogenase",

abstract = "To understand the molecular details of O2-tolerant hydrogen cycling by a soluble NAD+-reducing [NiFe] hydrogenase, we herein present the first bioinspired heterobimetallic S-oxygenated [NiFe] complex as a structural and vibrational spectroscopic model for the oxygen-inhibited [NiFe] active site. This compound and its non-S-oxygenated congener were fully characterized, and their electronic structures were elucidated in a combined experimental and theoretical study with emphasis on the bridging sulfenato moiety. Based on the vibrational spectroscopic properties of these complexes, we also propose novel strategies for exploring S-oxygenated intermediates in hydrogenases and similar enzymes.",

keywords = "enzyme models, IR spectroscopy, resonance Raman spectroscopy, spectroscopic models, [NiFe] hydrogenases",

author = "Lindenmaier, {Nils J.} and Stefan Wahlefeld and Eckhard Bill and Tibor Szilv{\'a}si and Christopher Eberle and Shenglai Yao and Peter Hildebrandt and Marius Horch and Ingo Zebger and Matthias Driess",

year = "2017",

month = jan,

day = "1",

doi = "10.1002/anie.201611069",

language = "English",

volume = "56",

pages = "2208--2211",

journal = "Angewandte Chemie - International Edition",

issn = "1433-7851",

publisher = "Wiley-Blackwell",

number = "8",

}

TY - JOUR

T1 - An S-Oxygenated [NiFe] Complex Modelling Sulfenate Intermediates of an O2-Tolerant Hydrogenase

AU - Lindenmaier, Nils J.

AU - Wahlefeld, Stefan

AU - Bill, Eckhard

AU - Szilvási, Tibor

AU - Eberle, Christopher

AU - Yao, Shenglai

AU - Hildebrandt, Peter

AU - Horch, Marius

AU - Zebger, Ingo

AU - Driess, Matthias

PY - 2017/1/1

Y1 - 2017/1/1

N2 - To understand the molecular details of O2-tolerant hydrogen cycling by a soluble NAD+-reducing [NiFe] hydrogenase, we herein present the first bioinspired heterobimetallic S-oxygenated [NiFe] complex as a structural and vibrational spectroscopic model for the oxygen-inhibited [NiFe] active site. This compound and its non-S-oxygenated congener were fully characterized, and their electronic structures were elucidated in a combined experimental and theoretical study with emphasis on the bridging sulfenato moiety. Based on the vibrational spectroscopic properties of these complexes, we also propose novel strategies for exploring S-oxygenated intermediates in hydrogenases and similar enzymes.

AB - To understand the molecular details of O2-tolerant hydrogen cycling by a soluble NAD+-reducing [NiFe] hydrogenase, we herein present the first bioinspired heterobimetallic S-oxygenated [NiFe] complex as a structural and vibrational spectroscopic model for the oxygen-inhibited [NiFe] active site. This compound and its non-S-oxygenated congener were fully characterized, and their electronic structures were elucidated in a combined experimental and theoretical study with emphasis on the bridging sulfenato moiety. Based on the vibrational spectroscopic properties of these complexes, we also propose novel strategies for exploring S-oxygenated intermediates in hydrogenases and similar enzymes.

KW - enzyme models

KW - IR spectroscopy

KW - resonance Raman spectroscopy

KW - spectroscopic models

KW - [NiFe] hydrogenases

UR - http://www.scopus.com/inward/record.url?scp=85009929114&partnerID=8YFLogxK

U2 - 10.1002/anie.201611069

DO - 10.1002/anie.201611069

M3 - Article

C2 - 28079958

AN - SCOPUS:85009929114

SN - 1433-7851

VL - 56

SP - 2208

EP - 2211

JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 8

ER -