[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 …

Heme protein assemblies

CJ Reedy, BR Gibney - Chemical reviews, 2004 - ACS Publications
Hemes remain one of the most visible and versatile classes of cofactors utilized in biology. 1
Since their discovery, the structural and functional aspects of heme proteins have fascinated …

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 …

A carbon dots-enhanced laccase-based electrochemical sensor for highly sensitive detection of dopamine in human serum

R Wu, S Yu, S Chen, Y Dang, SH Wen, J Tang… - Analytica Chimica …, 2022 - Elsevier
Enzyme-based electrochemical sensor possesses a significant advantage in the highly
efficient detection of small molecules, however, the poor electron transport efficiency limits …

An expandable, modular de novo protein platform for precision redox engineering

GH Hutchins, CEM Noble, HA Bunzel… - Proceedings of the …, 2023 - National Acad Sciences
The electron-conducting circuitry of life represents an as-yet untapped resource of exquisite,
nanoscale biomolecular engineering. Here, we report the characterization and structure of a …

Structure–function relationships in heme-proteins

M Paoli, J Marles-Wright, ANN Smith - DNA and cell biology, 2002 - liebertpub.com
Biological systems rely on heme-proteins to carry out a number of basic functions essential
for their survival. Hemes, or iron–porphyrin complexes, are the versatile and ubiquitous …

De novo proteins from designed combinatorial libraries

MH Hecht, A Das, A Go, LH Bradley, Y Wei - Protein Science, 2004 - Wiley Online Library
Combinatorial libraries of de novo amino acid sequences can provide a rich source of
diversity for the discovery of novel proteins with interesting and important activities …

Peptide-based heme− protein models

A Lombardi, F Nastri, V Pavone - Chemical reviews, 2001 - ACS Publications
Metalloproteins are involved in fundamental biological processes and utilize a relatively
small number of metal-based prosthetic groups to serve numerous and diverse chemical …

The redox protein construction kit: pre-last universal common ancestor evolution of energy-conserving enzymes

F Baymann, E Lebrun, M Brugna… - … of the Royal …, 2003 - royalsocietypublishing.org
Genome analyses and the resolution of three–dimensional structures have provided
evidence in recent years for hitherto unexpected family relationships between redox proteins …