Requirements for Cell-Free Cyanide Oxidation by Pseudomonas Fluorescens NCIMB 11764

PDF Version Also Available for Download.

Description

The involvement of cyanide oxygenase in the metabolism of pyruvate and a-ketoglutarate-cyanohydrin was investigated and shown to occur indirectly by the consumption of free cyanide arising from the cyanohydrins via chemical dissociation. Thus, free cyanide remains the substrate, for which the enzyme displays a remarkably high affinity (Kmapp,4 mM). A model for cyanide utilization is therefore envisioned in which the substrate is initially detoxified by complexation to an appropriate ligand followed by enzymatic oxidation of cyanide arising at sublethal levels via chemical dissociation. Putative cyanide oxygenase in cell extracts consumed both oxygen and NADH in equimolar proportions during cyanide conversion ... continued below

Creation Information

Parab, Preeti August 2000.

Context

This thesis is part of the collection entitled: UNT Theses and Dissertations and was provided by UNT Libraries to Digital Library, a digital repository hosted by the UNT Libraries. It has been viewed 355 times . More information about this thesis can be viewed below.

Who

People and organizations associated with either the creation of this thesis or its content.

Author

Chair

Committee Members

Publisher

Rights Holder

For guidance see Citations, Rights, Re-Use.

  • Parab, Preeti

Provided By

UNT Libraries

With locations on the Denton campus of the University of North Texas and one in Dallas, UNT Libraries serves the school and the community by providing access to physical and online collections; The Portal to Texas History and UNT Digital Libraries; academic research, and much, much more.

Contact Us

What

Descriptive information to help identify this thesis. Follow the links below to find similar items on the Digital Library.

Degree Information

Description

The involvement of cyanide oxygenase in the metabolism of pyruvate and a-ketoglutarate-cyanohydrin was investigated and shown to occur indirectly by the consumption of free cyanide arising from the cyanohydrins via chemical dissociation. Thus, free cyanide remains the substrate, for which the enzyme displays a remarkably high affinity (Kmapp,4 mM). A model for cyanide utilization is therefore envisioned in which the substrate is initially detoxified by complexation to an appropriate ligand followed by enzymatic oxidation of cyanide arising at sublethal levels via chemical dissociation. Putative cyanide oxygenase in cell extracts consumed both oxygen and NADH in equimolar proportions during cyanide conversion to CO2 and NH3 and existed separately from an unknown heat-stable species responsible for the nonenzymatic cyanide-catalyzed consumption of oxygen. Evidence of cyanide inhibition and nonlinear kinetics between enzyme activity and protein concentration point to a complex mechanism of enzymatic substrate conversion.

Subjects

Language

Identifier

Unique identifying numbers for this thesis in the Digital Library or other systems.

Collections

This thesis is part of the following collection of related materials.

UNT Theses and Dissertations

Theses and dissertations represent a wealth of scholarly and artistic content created by masters and doctoral students in the degree-seeking process. Some ETDs in this collection are restricted to use by the UNT community.

What responsibilities do I have when using this thesis?

When

Dates and time periods associated with this thesis.

Creation Date

  • August 2000

Added to The UNT Digital Library

  • Sept. 25, 2007, 9:03 p.m.

Description Last Updated

  • May 13, 2016, 6:43 p.m.

Usage Statistics

When was this thesis last used?

Yesterday: 0
Past 30 days: 2
Total Uses: 355

Interact With This Thesis

Here are some suggestions for what to do next.

Start Reading

PDF Version Also Available for Download.

Citations, Rights, Re-Use

Parab, Preeti. Requirements for Cell-Free Cyanide Oxidation by Pseudomonas Fluorescens NCIMB 11764, thesis, August 2000; Denton, Texas. (digital.library.unt.edu/ark:/67531/metadc2614/: accessed December 13, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; .