William Carl Kerstetter LPC/MHSP
Counselor/Therapist | Professional
218 EAST MAIN STREET MONTEAGLE TN, 37356About
William Kerstetter is a counselor in MONTEAGLE, TN. William evaluates patients using many different procedures, in order to determine what treatments must be carried out in order to properly assess their symptoms. Counselors provide consultation for each patient and their families.
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Expert Publications
Data provided by the National Library of Medicine- Electron-transfer mechanisms through biological redox chains in multicenter enzymes.
- Direct comparison of the electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalyst.
- Enzyme electrokinetics: hydrogen evolution and oxidation by Allochromatium vinosum [NiFe]-hydrogenase.
- Enzyme electrokinetics: electrochemical studies of the anaerobic interconversions between active and inactive states of Allochromatium vinosum [NiFe]-hydrogenase.
- Enzyme electrokinetics: using protein film voltammetry to investigate redox enzymes and their mechanisms.
- The role of the active site-coordinating cysteine residues in the maturation of the H2-sensing [NiFe] hydrogenase from Ralstonia eutropha H16.
- NiFe hydrogenase active site biosynthesis: identification of Hyp protein complexes in Ralstonia eutropha.
- [NiFe]-hydrogenases of Ralstonia eutropha H16: modular enzymes for oxygen-tolerant biological hydrogen oxidation.
- Synthetic hydrogenases: incorporation of an iron carbonyl thiolate into a designed peptide.
- Crystallization and preliminary X-ray crystallographic analysis of the [NiFe]-hydrogenase maturation factor HypF1 from Ralstonia eutropha H16.
- The [NiFe]-hydrogenase of the cyanobacterium Synechocystis sp. PCC 6803 works bidirectionally with a bias to H2 production.
- Spectroelectrochemistry of cytochrome c and azurin immobilized in nanoporous antimony-doped tin oxide.
- Transparent gold as a platform for adsorbed protein spectroelectrochemistry: investigation of cytochrome c and azurin.
- Biomimetic model for [FeFe]-hydrogenase: asymmetrically disubstituted diiron complex with a redox-active 2,2'-bipyridyl ligand.
- Sequential oxidations of thiolates and the cobalt metallocenter in a synthetic metallopeptide: implications for the biosynthesis of nitrile hydratase.
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