Cause and Effect of Dimer Asymmetry in Mercuric Reductas

Miller, Susan Mary

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of General Medical Sciences (NIGMS)
• Type: First Independent Research Support & Transition (FIRST) Awards (R29)
• Project #: 5R29GM050670-02
• Application #: 2188642
• Study Section: Physical Biochemistry Study Section (PB)
• Project Start: 1995-01-01
• Project End: 1999-12-31
• Budget Start: 1996-01-01
• Budget End: 1996-12-31
• Support Year: 2
• Fiscal Year: 1996

Institution

• Name: University of California San Francisco
• Department: Pharmacology
• Type: Schools of Pharmacy
• DUNS #: 073133571
• City: San Francisco
• State: CA
• Country: United States
• Zip Code: 94143

Publications

Engst, S; Miller, S M (1999) Alternative routes for entry of HgX2 into the active site of mercuric ion reductase depend on the nature of the X ligands. Biochemistry 38:3519-29

Miller, S M (1999) Bacterial detoxification of Hg(II) and organomercurials. Essays Biochem 34:17-30

Engst, S; Miller, S M (1998) Rapid reduction of Hg(II) by mercuric ion reductase does not require the conserved C-terminal cysteine pair using HgBr2 as the substrate. Biochemistry 37:11496-507

Miller, S M (1995) 2'-fluoro-2'-deoxy-D-arabinoflavin: characterization of a novel flavin and its effects on the formation and stability of two-electron-reduced mercuric ion reductase. Biochemistry 34:13066-73