Sergei V. Khangulov

Crystal Structure of Formate Dehydrogenase H: Catalysis Involving Mo, Molybdopterin, Selenocysteine, and an Fe4S4 Cluster (2007)

Boyington, Jeffrey C., Gladyshev, Vadim, Khangulov, Sergei V., Stadtman, Thressa C., Sun, Peter D.

Formate dehydrogenase H from Escherichia coli contains selenocysteine (SeCys), molybdenum, two molybdopterin guanine dinucleotide (MGD) cofactors, and an Fe4S4 cluster at the active site and...

Characterization of Crystalline Formate Dehydrogenase H from Escherichia coli (1996)

Gladyshev, Vadim N., Boyington, Jeffrey C., Khangulov, Sergei V., Grahame, David, Stadtman, Thressa C., Sun, Peter D.

The selenocysteine-containing formate dehydrogenase H (FDH) is an 80-kDa component of the Escherichia coli formate-hydrogen lyase complex. The molybdenumcoordinated selenocysteine is essential for...

Coordination of selenium to molybdenum in formate dehydrogenase H from Escherichia coli (1994)

Gladyshev, Vadim, Khangulov, Sergei V., Axley, Milton J., Stadtman, Thressa A.

Formate dehydrogenase H from Escherichia col contains multiple redox centers, which include a molybdopterin cofactor, an iron-sulfur center, and a selenocysteine residue (SeCys-140 in the polypeptide...

Nicotinic acid hydroxylase from Clostridium barkeri: Electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzymeNicotinic acid hydroxylase from Clostridium barkeri: Electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzyme (1994)

Gladyshev, Vadim, Khangulov, Sergei V., Stadtman, Thressa C.

Nicotinic acid hydroxylase from Clostidum barkeri contains selenium in an unidentified form that is dissociated as a low molecular weight compound upon denaturation of the enzyme. Other cofactors of...