Potentiometric CO titrations of carbon monoxide dehydrogenase and CO-inhibition of the NI-removing reaction with 1,10--phenanthroline /
(B.,, + e- = Bed) and a one-electron reduction and CO-
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| Format: | Thesis eBook |
| Language: | English |
| Published: |
[Place of publication not identified] :
[publisher not identified] ;
1996.
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| Subjects: | |
| Online Access: | Link to OAKTrust copy |
| Summary: | (B.,, + e- = Bed) and a one-electron reduction and CO- 2e- =C,,d2)(model 1) and a model that assumed two one- acetyl-CoA) using three types of Ni and Fe-S structures and CO2 atmospheres. The A, B, and C clusters EPR signals atmosphere. The saturation properties of the B cluster EPR atmosphere. The EPR signals of the A and C clusters also binding of the A-cluster (A.,, + e- + CO = A[ ]-CO). The C- called the A-, B-, and C-clusters. In this study, the enzyme Carbon monoxide dehydrogenase from Clostridium thermoaceticum catalyzes two reactions involving redox chemistry (the chelating it. However, other studies suggest that CO binds cluster was simulated using a two-electron reduction(Cedl + CO implies that CO binds this Ni and blocks phen from corresponding to the three clusters and the redox potential developed at much lower concentrations of CO in a C02 developed at potentials -250, 150, and 250 mV more Positive, e-= C[ ])(model 2). The development of EPR signals electron reductions of the C-cluster(C[ ] + e- = Cint and Cit of these clusters were found to be quite different under Ar phen indirectly should be considered. phenanthroline, with Ki = 840 atm-1. Since this reaction reductant and substrate CO, under Ar and C02 atmospheres, and respectively, under a C02 atmosphere relative to an Ar reversible oxidation Of CO to C02, and the synthesis of selectively removes the Ni from the A-cluster, inhibition by signal (g,,, = 1.94)changed significantly under C02. significance of the effect Of C02 is discussed. CO was found simulated assuming a one-electron reduction of the B-cluster spectroscopy (EPR). The resulting spectral changes were that C02 binding effects a conformational change that alters the enzyme's redox clusters. The possible catalytic the reduction potentials and electron transfer properties of then monitored by electron paramagnetic resonance These C02 effects confirm and strengthen a previous proposal to an Fe of the A-cluster, and the possibility that CO blocks to inhibit the reaction of the enzyme with 1, I 0- was incubated under various partial pressures of the |
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| Item Description: | "Major subject: Chemistry". In title, symbols are used. Vita. |
| Physical Description: | ix, 45 leaves : illustrations ; 28 cm. Also available online. Issued also on microfiche from Lange Micrographics. |
| Bibliography: | Includes bibliographical references: pages 42-44. |