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Part I. Coenzyme B₁₂ as a Hydroformylation-Type Catalyst. Part II. Mechanisms of Hydrogen Transfer in the Methylmalonyl Coenzyme A Mutase Reaction

Citation

Miller, William Walter (1968) Part I. Coenzyme B₁₂ as a Hydroformylation-Type Catalyst. Part II. Mechanisms of Hydrogen Transfer in the Methylmalonyl Coenzyme A Mutase Reaction. Dissertation (Ph.D.), California Institute of Technology. doi:10.7907/BBKP-QT89. https://resolver.caltech.edu/CaltechTHESIS:12182015-145538579

Abstract

Part I

The mechanism of the hydroformylation reaction was studied. Using cobalt deuterotetracarbonyl and 1-pentene as substrates, the first step in the reaction, addition of cobalt tetracarbonyl to an olefin, was shown to be reversible.

Part II

The role of coenzyme B12 in the isomerization of methylmalonyl coenzyme A to succinyl coenzyme A by methylmalonyl coenzyme A mutase was studied. The reaction was allowed to proceed to partial completion using a mixture of methylmalonyl coenzyme A and 4, 4, 4-tri-2H-methylmalonyl coenzyme A as substrate. The deuterium distribution in the product, succinyl coenzyme A, was shown to best fit a model in which hydrogen is transferred from C-4 of methylmalonyl coenzyme A to C-5’ of the adenosyl moiety of coenzyme B12 in the rate determining step. The three hydrogens at the 5’-adenosyl position of the coenzyme B12 intermediate are then able to become enzymatically equivalent before hydrogen is transferred from the coenzyme B12 intermediate to form succinyl coenzyme A.

Item Type:Thesis (Dissertation (Ph.D.))
Subject Keywords:(Chemistry)
Degree Grantor:California Institute of Technology
Division:Chemistry and Chemical Engineering
Major Option:Chemistry
Thesis Availability:Public (worldwide access)
Research Advisor(s):
  • Richards, John H.
Thesis Committee:
  • Unknown, Unknown
Defense Date:22 September 1967
Additional Information:Title varies in the 1968 Caltech commencement program: The Role of Coenzyme B12 in the Isomerization of Methylmalonyl Coenzyme A
Record Number:CaltechTHESIS:12182015-145538579
Persistent URL:https://resolver.caltech.edu/CaltechTHESIS:12182015-145538579
DOI:10.7907/BBKP-QT89
Default Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:9329
Collection:CaltechTHESIS
Deposited By:INVALID USER
Deposited On:21 Dec 2015 17:38
Last Modified:03 Apr 2024 23:40

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