[HTML][HTML] Metalloproteins containing cytochrome, iron–sulfur, or copper redox centers

J Liu, S Chakraborty, P Hosseinzadeh, Y Yu… - Chemical …, 2014 - ACS Publications
Redox reactions play important roles in almost all biological processes, including
photosynthesis and respiration, which are two essential energy processes that sustain all life …

Multifunctional Cytochrome c: Learning New Tricks from an Old Dog

D Alvarez-Paggi, L Hannibal, MA Castro… - Chemical …, 2017 - ACS Publications
Cytochrome c (cyt c) is a small soluble heme protein characterized by a relatively flexible
structure, particularly in the ferric form, such that it is able to sample a broad conformational …

Conformational control of cofactors in nature–the influence of protein-induced macrocycle distortion on the biological function of tetrapyrroles

MO Senge, SA MacGowan, JM O'Brien - Chemical Communications, 2015 - pubs.rsc.org
Tetrapyrrole-containing proteins are one of the most fundamental classes of enzymes in
nature and it remains an open question to give a chemical rationale for the multitude of …

Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics

P Hosseinzadeh, Y Lu - Biochimica et Biophysica Acta (BBA)-Bioenergetics, 2016 - Elsevier
Redox potentials are a major contributor in controlling the electron transfer (ET) rates and
thus regulating the ET processes in the bioenergetics. To maximize the efficiency of the ET …

Biological Significance and Applications of Heme c Proteins and Peptides

JG Kleingardner, KL Bren - Accounts of chemical research, 2015 - ACS Publications
Conspectus Hemes are ubiquitous in biology and carry out a wide range of functions. The
heme group is largely invariant across proteins with different functions, although there are a …

Spin cascade and doming in ferric hemes: Femtosecond X-ray absorption and X-ray emission studies

C Bacellar, D Kinschel, GF Mancini… - Proceedings of the …, 2020 - National Acad Sciences
The structure–function relationship is at the heart of biology, and major protein deformations
are correlated to specific functions. For ferrous heme proteins, doming is associated with the …

Heme–protein interactions and functional relevant heme deformations: the cytochrome c case

R Schweitzer-Stenner - Molecules, 2022 - mdpi.com
Heme proteins are known to perform a plethora of biologically important functions. This
article reviews work that has been conducted on various class I cytochrome c proteins over a …

Going with the Electron Flow: Heme Electronic Structure and Electron Transfer in Cytochrome c

KL Bren - Israel Journal of Chemistry, 2016 - Wiley Online Library
Heme is an essential and functionally versatile cofactor. Our understanding of how the
environment of a heme in a protein tunes its function has benefited from spectroscopic and …

The Influence of Heme Ruffling on Spin Densities in Ferricytochromes c Probed by Heme Core 13C NMR

JG Kleingardner, SEJ Bowman, KL Bren - Inorganic chemistry, 2013 - ACS Publications
The heme in cytochromes c undergoes a conserved out-of-plane distortion known as
ruffling. For cytochromes c from the bacteria Hydrogenobacter thermophilus and …

[HTML][HTML] Molecular mechanisms of electron transfer employed by native proteins and biological-inorganic hybrid systems

M Lienemann - Computational and Structural Biotechnology Journal, 2021 - Elsevier
Recent advances in enzymatic electrosynthesis of desired chemicals in biological-inorganic
hybrid systems has generated interest because it can use renewable energy inputs and …