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Review

Molecular Details on Multiple Cofactor Containing Redox Metalloproteins Revealed by Infrared and Resonance Raman Spectroscopies

1
Instituto de Tecnologia Química e Biológica António Xavier, Universidade NOVA de Lisboa, Av. da República, 2780-157 Oeiras, Portugal
2
Institut fur Chemie, Sekr. PC14, Technische Universitat Berlin, Strasse des 17. Juni 135, D-10623 Berlin, Germany
*
Author to whom correspondence should be addressed.
Academic Editors: Paola Taddei and Michele Di Foggia
Molecules 2021, 26(16), 4852; https://doi.org/10.3390/molecules26164852
Received: 12 July 2021 / Revised: 6 August 2021 / Accepted: 7 August 2021 / Published: 11 August 2021
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. View Full-Text
Keywords: vibrational spectroscopy; metalloproteins; resonance Raman spectroscopy; IR; heme proteins; Fe-S clusters; hydrogenases vibrational spectroscopy; metalloproteins; resonance Raman spectroscopy; IR; heme proteins; Fe-S clusters; hydrogenases
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MDPI and ACS Style

Silveira, C.M.; Zuccarello, L.; Barbosa, C.; Caserta, G.; Zebger, I.; Hildebrandt, P.; Todorovic, S. Molecular Details on Multiple Cofactor Containing Redox Metalloproteins Revealed by Infrared and Resonance Raman Spectroscopies. Molecules 2021, 26, 4852. https://doi.org/10.3390/molecules26164852

AMA Style

Silveira CM, Zuccarello L, Barbosa C, Caserta G, Zebger I, Hildebrandt P, Todorovic S. Molecular Details on Multiple Cofactor Containing Redox Metalloproteins Revealed by Infrared and Resonance Raman Spectroscopies. Molecules. 2021; 26(16):4852. https://doi.org/10.3390/molecules26164852

Chicago/Turabian Style

Silveira, Célia M., Lidia Zuccarello, Catarina Barbosa, Giorgio Caserta, Ingo Zebger, Peter Hildebrandt, and Smilja Todorovic. 2021. "Molecular Details on Multiple Cofactor Containing Redox Metalloproteins Revealed by Infrared and Resonance Raman Spectroscopies" Molecules 26, no. 16: 4852. https://doi.org/10.3390/molecules26164852

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