2ZAV

Crystal structure of human arginase I complexed with thiosemicarbazide reveals an unusual thiocarbonyl mu-sulfide ligand in the binuclear manganese cluster

(2007) J Am Chem Soc 129: 6388-6389

• PubMed: 17469833 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1021/ja071567j
• Primary Citation of Related Structures:  
  2PHA, 2PHO, 2ZAV


• PubMed Abstract: 
  

  The crystal structure of the human arginase I-thiosemicarbazide complex reveals an unusual thiocarbonyl μ-sulfide ligand in the binuclear manganese cluster. The C=S moiety of thiosemicarbazide bridges Mn ²⁺ A and Mn ²⁺ B with coordination distances of 2.6 ? and 2.4 ?, respectively. Otherwise, the binding of thiosemicarbazide to human arginase I does not cause any significant structural changes in the active site. The crystal structure of the unliganded enzyme reveals a hydrogen bonded water molecule that could support proton transfer between a μ-water molecule and H141 to regenerate the nucleophilic μ-hydroxide ion in the final step of catalysis.

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Organizational Affiliation: 

Roy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104-6323, USA.