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VALERIE DAVIDSON, DO
DO
Student in an Organized Health Care Education/Training Program
NPI: 1215519913Individual
Specialties, Licenses & Credentials
Student in an Organized Health Care Education/Training ProgramPrimary
Student in an Organized Health Care Education/Training Program
Code: 390200000X
Research & Publications (20)
Protein control of true, gated, and coupled electron transfer reactions.
PMID 18442271·Acc Chem Res·2008
8-other
Protein-derived cofactors. Expanding the scope of post-translational modifications.
PMID 17439161·Biochemistry·2007
6-review
Involvement of a putative [Fe-S]-cluster-binding protein in the biogenesis of quinohemoprotein amine dehydrogenase.
PMID 16546999·J Biol Chem·2006
8-other
Evidence for substrate activation of electron transfer from methylamine dehydrogenase to amicyanin.
PMID 12630872·J Am Chem Soc·2003
8-other
Probing mechanisms of catalysis and electron transfer by methylamine dehydrogenase by site-directed mutagenesis of alpha Phe55.
PMID 12686138·Biochim Biophys Acta·2003
6-review
Chemically gated electron transfer. A means of accelerating and regulating rates of biological electron transfer.
PMID 12475211·Biochemistry·2002
6-review
Lysozyme-osmotic shock methods for localization of periplasmic redox proteins in bacteria.
PMID 12078488·Methods Enzymol·2002
8-other
Pyrroloquinoline quinone (PQQ) from methanol dehydrogenase and tryptophan tryptophylquinone (TTQ) from methylamine dehydrogenase.
PMID 11665494·Adv Protein Chem·2001
6-review
Effects of kinetic coupling on experimentally determined electron transfer parameters.
PMID 10769151·Biochemistry·2000
8-other
Tyr(30) of amicyanin is not critical for electron transfer to cytochrome c-551i: implications for predicting electron transfer pathways.
PMID 10692547·Biochim Biophys Acta·2000
8-other
Methylamine dehydrogenase. Structure and function of electron transfer complexes.
PMID 11192720·Subcell Biochem·2000
6-review
What controls the rates of interprotein electron-transfer reactions.
PMID 10673316·Acc Chem Res·2000
6-review
A multifactorial risk prioritization framework for foodborne pathogens.
PMID 19671103·Risk Anal·2010
8-other
Kinetic mechanism for the initial steps in MauG-dependent tryptophan tryptophylquinone biosynthesis.
PMID 19196017·Biochemistry·2009
8-other
Uncovering novel biochemistry in the mechanism of tryptophan tryptophylquinone cofactor biosynthesis.
PMID 19648051·Curr Opin Chem Biol·2009
6-review
The axial ligand and extent of protein folding determine whether Zn or Cu binds to amicyanin.
PMID 17986390·J Inorg Biochem·2008
8-other
Kinetic and physical evidence that the diheme enzyme MauG tightly binds to a biosynthetic precursor of methylamine dehydrogenase with incompletely formed tryptophan tryptophylquinone.
PMID 18220357·Biochemistry·2008
8-other
A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical.
PMID 18562294·Proc Natl Acad Sci U S A·2008
8-other
Data courtesy of the U.S. National Library of Medicine (NLM). Ltrl is not affiliated with or endorsed by NLM.
Contact & Hours
- Address
- 22101 MOROSS RD
DETROIT, MI 48236 - Phone
- (313) 343-7110
Quick Facts
- NPI
- 1215519913
- Entity Type
- Individual
- Gender
- Female
- Medicare
- Not confirmed
- Specialties
- 1
- Locations
- 1
- Publications
- 20
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