Protein science : a publication of the Protein Society.
Publisher:
Cambridge University Press,. Woodbury, NY : Cold Spring Harbor Laboratory Press (2001)
Frequency: Monthly
Country: United States
Language: English
Author(s):
Protein Society., American Society for Biochemistry and Molecular Biology., Innovative Technology Fund.
Start Year:1992 -
ISSN:
0961-8368 (Print)
1469-896X (Electronic)
0961-8368 (Linking)
1469-896X (Electronic)
0961-8368 (Linking)
Impact Factor
8
2022
| NLM ID: | 9211750 |
| (DNLM): | SR0070820(s) |
| (OCoLC): | 25450084 |
| Coden: | PRCIEI |
| Classification: | W1 PR788J |
The redox couple of the cytochrome c cyanide complex: the contribution of heme iron ligation to the structural stability, chemical reactivity, and physiological behavior of horse cytochrome c. Contrary to most heme proteins, ferrous cytochrome c does not bind ligands such as cyanide and CO. In order to quantify this observation, the redox potential of the ferric/ferrous cytochrome c-cyanide redox couple was determined for the first time by cyclic voltammetry. Its E0' was -240 mV versus SHE, equivalent to -23.2 kJ/mol. The entropy of reaction for the reduction of the cyanide complex was also determined. From a thermodynamic cycle that included this new value for the cyt c cyanide complex E0', the binding constant of cyanide to the reduced protein was estimated to be 4.7 x 10(-3) L M(...
Structure of equine infectious anemia virus proteinase complexed with an inhibitor. Equine infectious anemia virus (EIAV), the causative agent of infectious anemia in horses, is a member of the lentiviral family. The virus-encoded proteinase (PR) processes viral polyproteins into functional molecules during replication and it also cleaves viral nucleocapsid protein during infection. The X-ray structure of a complex of the 154G mutant of EIAV PR with the inhibitor HBY-793 was solved at 1.8 A resolution and refined to a crystallographic R-factor of 0.136. The molecule is a dimer in which the monomers are related by a crystallographic twofold axis. Although both the enzyme and t...
Volume changes of the molten globule transitions of horse heart ferricytochrome c: a thermodynamic cycle. Volume changes among the unfolded (U), native (N), and molten globule (MG) conformations of horse heart ferricytochrome c have been measured. U to N (pH 2 to pH 7) was determined in the absence of added salt to be -136 +/- 5 mL/mol protein. U to MG (pH 2, no added salt to pH 2, 0.5 M KCl) yielded + 100 +/- 6 mL/mol. MG to N was broken into two steps, N to NClx at pH 7 by addition of buffered KCl to buffered protein lacking added salt (NClx = N interacting with an unknown number, X, of chloride ions), and MG to NClx by jumping MG at pH 2 in 0.5 M KCl to pH7 at the same salt concentration. The d...