Epernicus: T Conn Mallett, Ph.D.

T Conn Mallett, Ph.D.

Position:
Scientific and Technical Operations Manager

Rigaku Europe
Degrees:

Ph.D., Biochemistry, Wake Forest University (Winston-Salem, NC)

B.S., Biochemistry, Virginia Tech (Blacksburg, VA)
Past Advisors:

Tomitake Tsukihara (as Post Doctoral Fellow)

Al Claiborne (as Graduate Student - Ph.D.)

Walter Niehaus (as Undergraduate Student)
Research:
To advance accessibility of structural biology instrumentation, techniques and methods to the general user community

Rigaku Europe:

Customer service management and administration focused on testing, documentation and scientist training in the use of Rigaku X-ray generators, optics, detectors, sample changing robots and ancillary devices.

Wake Forest University:

Structural and mechanistic studies of flavoprotein oxidases, peroxidases and disulfide reductases, focused on enzymes of the glutathione reductase class containing a single redox active cysteine at the active site including NADH oxidase, NADH peroxidase, and Coenzyme A Disulfide Reductase.
Other Experience:
2006-2007 Senior Application Scientist - Rigaku Europe

2001-2006 Assistant Professor of Biochemistry - Wake Forest University

Communities:

T Mallett's Genealogy

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T Mallett's Publications (14)

Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of dual NAD(P)H specificity.
Wallen JR, Paige C, Mallett TC, Karplus PA, Claiborne A

Biochemistry. 2008 May 6;47(18):5182-93
Structure of alpha-glycerophosphate oxidase from Streptococcus sp.: a template for the mitochondrial alpha-glycerophosphate dehydrogenase.
Colussi T, Parsonage D, Boles W, Matsuoka T, Mallett TC, Karplus PA, Claiborne A

Biochemistry. 2008 Jan 22;47(3):965-77
Structure of the type III pantothenate kinase from Bacillus anthracis at 2.0 A resolution: implications for coenzyme A-dependent redox biology.
Nicely NI, Parsonage D, Paige C, Newton GL, Fahey RC, Leonardi R, Jackowski S, Mallett TC, Claiborne A

Biochemistry. 2007 Mar 20;46(11):3234-45
Structure of coenzyme A-disulfide reductase from Staphylococcus aureus at 1.54 A resolution.
Mallett TC, Wallen JR, Karplus PA, Sakai H, Tsukihara T, Claiborne A

Biochemistry. 2006 Sep 26;45(38):11278-89
Crystallization and preliminary X-ray crystallographic studies of the alkanesulfonate FMN reductase from Escherichia coli.
Gao B, Bertrand A, Boles WH, Ellis HR, Mallett TC

Acta crystallographica. Section F, Structural biology and crystallization communications. 2005 Sep 1;61(Pt 9):837-40
Discovery and characterization of a Coenzyme A disulfide reductase from Pyrococcus horikoshii. Implications for this disulfide metabolism of anaerobic hyperthermophiles.
Harris DR, Ward DE, Feasel JM, Lancaster KM, Murphy RD, Mallet TC, Crane EJ

The FEBS journal. 2005 Mar;272(5):1189-200
Ligand binding promotes the entropy-driven oligomerization of integrin alpha IIb beta 3.
Hantgan RR, Lyles DS, Mallett TC, Rocco M, Nagaswami C, Weisel JW

The Journal of biological chemistry. 2003 Jan 31;278(5):3417-26
Structural, redox, and mechanistic parameters for cysteine-sulfenic acid function in catalysis and regulation.
Claiborne A, Mallett TC, Yeh JI, Luba J, Parsonage D

Advances in protein chemistry. 2001;58:215-76
Contribution of NADH oxidase to aerobic metabolism of Streptococcus pyogenes.
Gibson CM, Mallett TC, Claiborne A, Caparon MG

Journal of bacteriology. 2000 Jan;182(2):448-55
Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation.
Claiborne A, Yeh JI, Mallett TC, Luba J, Crane EJ, Charrier V, Parsonage D

Biochemistry. 1999 Nov 23;38(47):15407-16
Equilibrium analyses of the active-site asymmetry in enterococcal NADH oxidase: role of the cysteine-sulfenic acid redox center.
Mallett TC, Parsonage D, Claiborne A

Biochemistry. 1999 Mar 9;38(10):3000-11
The soluble alpha-glycerophosphate oxidase from Enterococcus casseliflavus. Sequence homology with the membrane-associated dehydrogenase and kinetic analysis of the recombinant enzyme.
Parsonage D, Luba J, Mallett TC, Claiborne A

The Journal of biological chemistry. 1998 Sep 11;273(37):23812-22
Oxygen reactivity of an NADH oxidase C42S mutant: evidence for a C(4a)-peroxyflavin intermediate and a rate-limiting conformational change.
Mallett TC, Claiborne A

Biochemistry. 1998 Jun 16;37(24):8790-802
Purification and characterization of glucose-6-phosphate dehydrogenase from Cryptococcus neoformans: identification as "nothing dehydrogenase".
Niehaus WG, Mallett TC

Archives of biochemistry and biophysics. 1994 Sep;313(2):304-9

One Figure

Reduced form of Coenzyme A-Disulfide Reductase in complex with NADH

Websites

Rigaku

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