Please use this identifier to cite or link to this item: http://dx.doi.org/10.14279/depositonce-12371
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Main Title: Molecular Details on Multiple Cofactor Containing Redox Metalloproteins Revealed by Infrared and Resonance Raman Spectroscopies
Author(s): Silveira, Célia M.
Zuccarello, Lidia
Barbosa, Catarina
Caserta, Giorgio
Zebger, Ingo
Hildebrandt, Peter
Todorovic, Smilja
Type: Article
Language Code: en
Abstract: Vibrational spectroscopy and in particular, resonance Raman (RR) spectroscopy, can provide molecular details on metalloproteins containing multiple cofactors, which are often challenging for other spectroscopies. Due to distinct spectroscopic fingerprints, RR spectroscopy has a unique capacity to monitor simultaneously and independently different metal cofactors that can have particular roles in metalloproteins. These include e.g., (i) different types of hemes, for instance hemes c, a and a3 in caa3-type oxygen reductases, (ii) distinct spin populations, such as electron transfer (ET) low-spin (LS) and catalytic high-spin (HS) hemes in nitrite reductases, (iii) different types of Fe-S clusters, such as 3Fe-4S and 4Fe-4S centers in di-cluster ferredoxins, and (iv) bi-metallic center and ET Fe-S clusters in hydrogenases. IR spectroscopy can provide unmatched molecular details on specific enzymes like hydrogenases that possess catalytic centers coordinated by CO and CN− ligands, which exhibit spectrally well separated IR bands. This article reviews the work on metalloproteins for which vibrational spectroscopy has ensured advances in understanding structural and mechanistic properties, including multiple heme-containing proteins, such as nitrite reductases that house a notable total of 28 hemes in a functional unit, respiratory chain complexes, and hydrogenases that carry out the most fundamental functions in cells.
URI: https://depositonce.tu-berlin.de/handle/11303/13584
http://dx.doi.org/10.14279/depositonce-12371
Issue Date: 11-Aug-2021
Date Available: 14-Sep-2021
DDC Class: 540 Chemie und zugeordnete Wissenschaften
Subject(s): vibrational spectroscopy
metalloproteins
resonance Raman spectroscopy
IR
heme proteins
Fe-S clusters
hydrogenases
Sponsor/Funder: DFG, 390540038, EXC 2008: Unifying Systems in Catalysis "UniSysCat"
EC/H2020/810856/EU/Twin to Illuminate Metals in Biology and Biocatalysis through Biospectroscopy/TIMB3
License: https://creativecommons.org/licenses/by/4.0/
Journal Title: Molecules
Publisher: MDPI
Publisher Place: Basel
Volume: 26
Issue: 16
Article Number: 4852
Publisher DOI: 10.3390/molecules26164852
EISSN: 1420-3049
Appears in Collections:FG Physikalische Chemie / Biophysikalische Chemie » Publications

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