[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 …

The role of key residues in structure, function, and stability of cytochrome-c

S Zaidi, MI Hassan, A Islam, F Ahmad - Cellular and molecular life …, 2014 - Springer
Abstract Cytochrome-c (cyt-c), a multi-functional protein, plays a significant role in the
electron transport chain, and thus is indispensable in the energy-production process …

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 …

Structure, functional characterization, and evolution of the dihydroorotase domain of human CAD

A Grande-García, N Lallous, C Díaz-Tejada… - Structure, 2014 - cell.com
Upregulation of CAD, the multifunctional protein that initiates and controls the de novo
biosynthesis of pyrimidines in animals, is essential for cell proliferation. Deciphering the …

The enthalpic and entropic terms of the reduction potential of metalloproteins: Determinants and interplay

G Di Rocco, G Battistuzzi, M Borsari… - Coordination Chemistry …, 2021 - Elsevier
Splitting the reduction potential of electron transport (ET) proteins and redox
metalloenzymes into the enthalpic and entropic contributions is an insightful practice to …

The good, the neutral, and the positive: buffer identity impacts CO 2 reduction activity by nickel (II) cyclam

CR Schneider, LC Lewis, HS Shafaat - Dalton Transactions, 2019 - pubs.rsc.org
Development of new synthetic catalysts for CO2 reduction has been a central focus of
chemical research efforts towards mitigating rising global carbon dioxide levels. In parallel …

Tuning the Fe (II/III) redox potential in nonheme Fe (II)–hydroxo complexes through primary and secondary coordination sphere modifications

Z Gordon, MJ Drummond, EM Matson… - Inorganic …, 2017 - ACS Publications
The derivatization of the imino-functionalized tris (pyrrolylmethyl) amine ligand framework, N
(XpiR) 3 (XLR; X= H, Br; R= cyclohexyl (Cy), phenyl (Ph), 2, 6-diisopropylphenyl (DIPP)), is …