Structure of the soluble domain of cytochrome c552 from Paracoccus denitrificans in the oxidized and reduced states
A Harrenga, B Reincke, H Rüterjans, B Ludwig… - Journal of Molecular …, 2000 - Elsevier
The crystal structure of the soluble domain of the membrane bound cytochrome c552
(cytochrome c552′) from Paracoccus denitrificans was determined using the …
(cytochrome c552′) from Paracoccus denitrificans was determined using the …
Solution structure of the functional domain of Paracoccus denitrificans cytochrome c552 in the reduced state
P Pristovšek, C Lücke, B Reincke… - European Journal of …, 2000 - Wiley Online Library
In order to determine the solution structure of Paracoccus denitrificans cytochrome c552 by
NMR, we cloned and isotopically labeled a 10.5‐kDa soluble fragment (100 residues) …
NMR, we cloned and isotopically labeled a 10.5‐kDa soluble fragment (100 residues) …
Redox-related conformational changes in Rhodobacter capsulatus cytochrome c2
D Zhao, HM Hutton, PR Gooley, NE Mackenzie… - Protein …, 2000 - cambridge.org
WEFT-NOESY and transfer WEFT-NOESY NMR spectra were used to determine the heme
proton assignments for Rhodobacter capsulatus ferricytochrome c2. The Fermi contact and …
proton assignments for Rhodobacter capsulatus ferricytochrome c2. The Fermi contact and …
A Membrane‐Bound Cytochrome c3: A Type II Cytochrome c3 from Desulfovibrio vulgaris Hildenborough
FMA Valente, LM Saraiva, J LeGall, AV Xavier… - …, 2001 - Wiley Online Library
A new tetraheme cytochrome c3 was isolated from the membranes of Desulfovibrio vulgaris
Hildenborough (DvH). This cytochrome has a molecular mass of 13.4 kDa and a pI of 5.5 …
Hildenborough (DvH). This cytochrome has a molecular mass of 13.4 kDa and a pI of 5.5 …
[HTML][HTML] Solution structures of tetrahaem ferricytochrome c3 from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: The molecular basis of cooperativity
AC Messias, AP Aguiar, L Brennan… - … et Biophysica Acta (BBA …, 2006 - Elsevier
The NMR structure of the oxidised wild-type cytochrome c3 from Desulfovibrio vulgaris
Hildenborough was determined in solution. Using a newly developed methodology, NMR …
Hildenborough was determined in solution. Using a newly developed methodology, NMR …
Relationship between Redox Function and Protein Stability of Cytochromes c
N Terui, N Tachiiri, H Matsuo, J Hasegawa… - Journal of the …, 2003 - ACS Publications
Electrochemical, 1H NMR, and optical studies on mesophile Pseudomonas aeruginosa
cytochrome c 551, its single (F34Y) and quintuple (F7A/V13M/F34Y/E43Y/V78I) mutants …
cytochrome c 551, its single (F34Y) and quintuple (F7A/V13M/F34Y/E43Y/V78I) mutants …
Substitutions engineered by chemical synthesis at three conserved sites in mitochondrial cytochrome c: Thermodynamic and functional consequences
CJA Wallace, P Mascagni, BT Chait, JF Collawn… - Journal of Biological …, 1989 - ASBMB
Analogues of the 39-residue CNBr fragment of horse cytochrome c (66–104) have been
prepared by total chemical synthesis. Conformationally assisted ligation of these peptides …
prepared by total chemical synthesis. Conformationally assisted ligation of these peptides …
The effect of replacing the axial methionine ligand with a lysine residue in cytochrome c‐550 from Paracoccus versutus assessed by X‐ray crystallography and …
JAR Worrall, AMM van Roon, M Ubbink… - The FEBS …, 2005 - Wiley Online Library
The structure of cytochrome c‐550 from the nonphotosynthetic bacteria Paraccocus versutus
has been solved by X‐ray crystallography to 1.90 Å resolution, and reveals a high structural …
has been solved by X‐ray crystallography to 1.90 Å resolution, and reveals a high structural …
[HTML][HTML] Cloning, expression, and physicochemical characterization of a new diheme cytochrome c from Shewanella baltica OS155
The 16-kDa diheme cytochrome c from the bacterium Shewanella baltica OS155 (Sb-DHC)
was cloned and expressed in Escherichia coli and investigated through UV–vis, magnetic …
was cloned and expressed in Escherichia coli and investigated through UV–vis, magnetic …
Design and Synthesis of de Novo Cytochromes c
Natural c-type cytochromes are characterized by the consensus Cys-XX-Cys-His heme-
binding motif (where X is any amino acid) by which the heme is covalently attached to …
binding motif (where X is any amino acid) by which the heme is covalently attached to …