Παρακαλώ χρησιμοποιήστε αυτό το αναγνωριστικό για να παραπέμψετε ή να δημιουργήσετε σύνδεσμο προς αυτό το τεκμήριο: https://hdl.handle.net/20.500.14279/1474
Τίτλος: The role of the cross-link His-Tyr in the functional properties of the binuclear center in cytochrome c oxidase
Συγγραφείς: Pinakoulaki, Eftychia 
Pfitzner, Ute 
Varotsis, Constantinos 
metadata.dc.contributor.other: Πινακουλάκη, Ευτυχία
Βαρώτσης, Κωνσταντίνος
Major Field of Science: Natural Sciences
Field Category: Chemical Sciences
Λέξεις-κλειδιά: Biochemistry;Enzymes;Infrared spectroscopy;Resonance;Carbon;Copper;Cytochrome oxidase;Protein binding;Raman spectrometry
Ημερομηνία Έκδοσης: 19-Απρ-2002
Πηγή: Journal of biological chemistry, 2002, vol. 277, no. 16, pp. 13563-13568
Volume: 277
Issue: 16
Start page: 13563
End page: 13568
Περιοδικό: Journal of Biological Chemistry 
Περίληψη: Resonance Raman and Fourier transform infrared spectroscopies have been used to study the aa3-type cytochrome c oxidase and the Y280H mutant from Paracoccus denitrificans. The stability of the binuclear center in the absence of the Tyr280-HiS276 cross-link is not compromised since heme a3 retains the same proximal environment, spin, and coordination state as in the wild type enzyme in both the oxidized and reduced states. We observe two C-O modes in the Y280H mutant at 1966 and 1975 cm-1. The 1975 cm-1 mode is assigned to a γ-form and represents a structure of the active site in which CuB exerts a steric effect on the heme a3-bound CO. Therefore, the role of the cross-link is to fix CuB in a certain configuration and distance from heme a3, and not to allow histidine ligands to coordinate to CuB rather than to heme a3, rendering the enzyme inactive, as proposed recently (Das, T. K., Pecoraro, C., Tomson, F. L., Gennis, R. B., and Rousseau, D. L. (1998) Biochemistry 37, 14471-14476). The results provide solid evidence that in the Y280H mutant the catalytic site retains its active configuration that allows O2 binding to heme a3. Oxygenated intermediates are formed by mixing oxygen with the CO-bound mixed-valence wild type and Y280H enzymes with similar Soret maxima at 438 nm
URI: https://hdl.handle.net/20.500.14279/1474
ISSN: 00219258
DOI: 10.1074/jbc.M112200200
Rights: © The American Society for Biochemistry and Molecular Biology, Inc
Attribution-NonCommercial-NoDerivs 3.0 United States
Type: Article
Affiliation: University of Crete 
Publication Type: Peer Reviewed
Εμφανίζεται στις συλλογές:Άρθρα/Articles

CORE Recommender
Δείξε την πλήρη περιγραφή του τεκμηρίου

SCOPUSTM   
Citations

76
checked on 9 Νοε 2023

WEB OF SCIENCETM
Citations

73
Last Week
0
Last month
0
checked on 29 Οκτ 2023

Page view(s) 20

499
Last Week
1
Last month
2
checked on 22 Δεκ 2024

Google ScholarTM

Check

Altmetric


Αυτό το τεκμήριο προστατεύεται από άδεια Άδεια Creative Commons Creative Commons