Coordination Dynamics of Zinc in Proteins

Abstract

Wolfgang Maret received his diploma in chemistry (1977) and his Ph.D. in natural sciences (1980) from the Saarland University, Saarbruecken, Germany. The mentor for his Ph.D. thesis on metal substitution in liver alcohol dehydrogenase was Prof. Michael Zeppezauer. During his postdoctoral years in Prof. Marvin W. Makinen's laboratory at the University of Chicago (1980-1982), he continued his education in mechanistic enzymology and spectroscopy. He joined Prof. Bert L. Vallee's Center for Biochemical and Biophysical Sciences and Medicine at Harvard Medical School as an assistant professor in 1986 and began to work on the chemical and biochemical mechanisms of cellular zinc homeostasis. Since 2003, Dr. Maret has been an associate professor in the Division of Human Nutrition (Department of Preventive Medicine and Community Health) at the University of Texas Medical Branch in Galveston, TX. His work focuses on molecular mechanisms of cellular metal homeostasis, sulfur redox chemistry, structure and function of metalloenzymes, and functions of micronutrients in chronic and degenerative diseases.

Zinc in Infection and Inflammation

“…Zinc research has come a long way since then; its significance as a structural component in many proteins and its participation in numerous cellular functions is now well established. Such functions include but not limited to cell proliferation and differentiation [2], RNA and DNA synthesis [3], as well as cell structures and cell membrane stabilization [4]. Its multifaceted role in the regulation of the immune system is particularly interesting and will be discussed in more detail in this review [5].…”

A novel small molecule fluorescent sensor for Zn2+ based on pyridine–pyridone scaffold

“…Zinc is an essential element for life and is known to play important roles in biological processes including gene expression, apoptosis, enzyme regulation, immune system and neurotransmission [1][2][3][4][5][6].…”

Trinuclear zinc complexes for biologically relevant μ3-oxoanion binding and carbon dioxide fixation

“…The zinc cation has key roles in enzymatic activity, structural organization and functional regulation due to its strong Lewis acidity and other unusual chemical properties, including rapid ligand exchange, flexible coordination and lack of redox chemistry under physiological conditions 4 . However, the physical properties of Zn(II) make most spectroscopic techniques and methodologies employed for probing other biological metals inapplicable to the characterization of zinc enzymes 2,4 .…”

“…The zinc cation has key roles in enzymatic activity, structural organization and functional regulation due to its strong Lewis acidity and other unusual chemical properties, including rapid ligand exchange, flexible coordination and lack of redox chemistry under physiological conditions 4 . However, the physical properties of Zn(II) make most spectroscopic techniques and methodologies employed for probing other biological metals inapplicable to the characterization of zinc enzymes 2,4 . Synthetic zinc models have attracted much attention [5][6][7][8][9][10][11] because they are more amenable to structural, spectroscopic and mechanistic studies that could provide information regarding zinc chemistry and its coordination environment 12,13 .…”

“…The conversion of CO 2 to carbonate is an important biological process catalysed by carbonic anhydrases that transports CO 2 out of tissues, maintains the acid-base balance and provides a biosynthetic carbon source 4,5,7,13 . Many synthetic efforts have been focused on mimicking this class of zinc enzymes 5,7,8,13,20 .…”