Document Detail

Circular dichroism of cobaltous complexes of creatine kinase.
MedLine Citation:
PMID:  921939     Owner:  NLM     Status:  MEDLINE    
Circular dichroic spectra in the visible wavelength region were used to investigate the local environment of Co(II), an activating metal, at the active site of rabbit muscle creatine kinase. There was a small spectral change when CoADP- was bound to creatine kinase, no change when creatine was added, and another small change when NO3- was added to form the transition state analogue. Using matrix rank analysis to quantitate these small spectral changes, a titratable group with a pK = 7.4 was found which modified the enzyme-bound metal-nucleotide interaction. These data suggest that, throughout the enzyme's catalysis, the metal-nucleotide interaction remains very similar in structure to the complex not bound to the enzyme.
J L Gabriel; R C Davis
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemistry     Volume:  16     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1977 Nov 
Date Detail:
Created Date:  1978-01-27     Completed Date:  1978-01-27     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  5364-7     Citation Subset:  IM    
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MeSH Terms
Adenosine Diphosphate
Circular Dichroism
Creatine Kinase*
Muscles / enzymology
Protein Binding
Protein Conformation
Reg. No./Substance:
58-64-0/Adenosine Diphosphate; 7440-48-4/Cobalt; EC Kinase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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