Russell R. Poyner

Chelation of Serine 39 to Mg2+ Latches a Gate at the Active Site of Enolase: Structure of the Bis(Mg2+) Complex of Yeast Enolase and the Intermediate Analog Phosphonoacetohydroxamate at 2.1-.ANG. Resolution

Joseph E. Wedekind, Russell R. Poyner, George H. Reed et al. · Biochemistry · 1994 · 95 citations

X-ray Coordinates, New Crystal Form, Cellular Enzymology +14

Toward Identification of Acid/Base Catalysts in the Active Site of Enolase:  Comparison of the Properties of K345A, E168Q, and E211Q Variants

Russell R. Poyner, L. Timothy Laughlin, Gwendolyn A. Sowa et al. · Biochemistry · 1996 · 65 citations

Structure of the bis divalent cation complex with phosphonoacetohydroxamate at the active site of enolase

Russell R. Poyner, George H. Reed · Biochemistry · 1992 · 45 citations

Role of Metal Ions in Catalysis by Enolase:  An Ordered Kinetic Mechanism for a Single Substrate Enzyme

Russell R. Poyner, W. W. Cleland, George H. Reed · Biochemistry · 2001 · 44 citations

Reverse Protonation Is the Key to General Acid−Base Catalysis in Enolase^,

Paul A. Sims, Todd M. Larsen, Russell R. Poyner et al. · Biochemistry · 2003 · 37 citations

Wild-type Enolase, Exchange Reaction, Engineering +15