Circular dichroism of cobalt (II) fructose-1, 6-bisphosphatase, 1977

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Title: Circular dichroism of cobalt (II) fructose-1, 6-bisphosphatase, 1977
Author: Dasher, David
Date: 1977-05-01
Decade: 1970-1979
Abstract: Chromophoric metal ions at the active site of metallo- enzymes are well known to participate in enzymatic catalysis and to be capable of serving as optical probes at the cation binding site. Cobalt(II) can be substituted at the cation binding site of fructose-1,6-bisphosphatase to form an active metalloenzyme. The complex formed gives rise to Circular Dichroism spectra responsive to such factors as changes in hydrogen ion concentration, substrate and/or inhibitor binding. The results of the measurement of these spectral properties of the Co(II) FbPase complex provides a specific example of the general relationship between spectra of chromophoric metal ions and the existence of irregular geometries for the enzyme cation binding site.
Document Type: text
Format: application/pdf
Date of Award: 1977-05-01
Degree Type: thesis
Degree Name: Master of Science (MS)
Granting Institution: Atlanta University
Department: Department of Chemistry
Advisor: Johnson, Joe
Owen, G. Scott
Institution: Clark Atlanta University
Geographic Location: Georgia--Atlanta
Handle: http://hdl.handle.net/20.500.12322/cau.td:1977_dasher_david
Rights Statement: http://rightsstatements.org/vocab/InC-EDU/1.0/