[HTML][HTML] Metalloproteins containing cytochrome, iron–sulfur, or copper redox centers
Redox reactions play important roles in almost all biological processes, including
photosynthesis and respiration, which are two essential energy processes that sustain all life …
photosynthesis and respiration, which are two essential energy processes that sustain all life …
How biology handles nitrite
Nitrite is one of the players in the broad nitrogen biogeochemical cycle. This nitrogen oxo-
anion is involved in key pathways crucial to life on Earth and to the planetary “recycling” of …
anion is involved in key pathways crucial to life on Earth and to the planetary “recycling” of …
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 …
nature and it remains an open question to give a chemical rationale for the multitude of …
Engineering novel metalloproteins: design of metal-binding sites into native protein scaffolds
Y Lu, SM Berry, TD Pfister - Chemical reviews, 2001 - ACS Publications
Proteins play an essential role in biology. Whether it is in catalysis or molecular recognition,
proteins set a golden standard of efficiency and selectivity that few other natural or artificial …
proteins set a golden standard of efficiency and selectivity that few other natural or artificial …
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 …
for their survival. Hemes, or iron–porphyrin complexes, are the versatile and ubiquitous …
Heme redox potential control in de novo designed four-α-helix bundle proteins
JM Shifman, BR Gibney, RE Sharp, PL Dutton - Biochemistry, 2000 - ACS Publications
The effects of various mechanisms of metalloporphyrin reduction potential modulation were
investigated experimentally using a robust, well-characterized heme protein maquette …
investigated experimentally using a robust, well-characterized heme protein maquette …
The hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough encodes a potential transmembrane redox protein complex
M Rossi, WB Pollock, MW Reij, RG Keon… - Journal of …, 1993 - Am Soc Microbiol
The nucleotide sequence of the hmc operon from Desulfovibrio vulgaris subsp. vulgaris
Hildenborough indicated the presence of eight open reading frames, encoding proteins Orf1 …
Hildenborough indicated the presence of eight open reading frames, encoding proteins Orf1 …
Analysis of the electrochemistry of hemes with Ems spanning 800 mV
The free energy of heme reduction in different proteins is found to vary over more than 18
kcal/mol. It is a challenge to determine how proteins manage to achieve this enormous …
kcal/mol. It is a challenge to determine how proteins manage to achieve this enormous …
Family of Cytochrome c7-Type Proteins from Geobacter sulfurreducens: Structure of One Cytochrome c7 at 1.45 Å Resolution,
PR Pokkuluri, YY Londer, NEC Duke, WC Long… - Biochemistry, 2004 - ACS Publications
The structure of a cytochrome c 7 (PpcA) from Geobacter sulfurreducens was determined by
X-ray diffraction at 1.45 Å resolution; the R factor is 18.2%. The protein contains a three …
X-ray diffraction at 1.45 Å resolution; the R factor is 18.2%. The protein contains a three …
The Structural Origin of Nonplanar Heme Distortions in Tetraheme Ferricytochromes c3
Resonance Raman (RR) spectroscopy, molecular mechanics (MM) calculations, and normal-
coordinate structural decomposition (NSD) have been used to investigate the …
coordinate structural decomposition (NSD) have been used to investigate the …