910561-65-8Relevant academic research and scientific papers
How does single oxygen atom addition affect the properties of an Fe-Nitrile hydratase analogue? The compensatory role of the unmodified thiolate
Lugo-Mas, Priscilla,Dey, Abhishek,Xu, Liang,Davin, Steven D.,Benedict, Jason,Kaminsky, Werner,Hodgson, Keith O.,Hedman, Britt,Solomon, Edward I.,Kovacs, Julie A.
, p. 11211 - 11221 (2006)
Nitrile hydratase (NHase) is one of a growing number of enzymes shown to contain posttranslationally modified cysteine sulfenic acids (Cys-SOH). Cysteine sulfenic acids have been shown to play diverse roles in cellular processes, including transcriptional regulation, signal transduction, and the regulation of oxygen metabolism and oxidative stress responses. The function of the cysteine sulfenic acid coordinated to the iron active site of NHase is unknown. Herein we report the first example of a sulfenate-ligated iron complex, [Fe III(ADIT)(ADIT-O)]+ (5), and compare its electronic and magnetic properties with those of structurally related complexes in which the sulfur oxidation state and protonation state have been systematically altered. Oxygen atom addition was found to decrease the unmodified thiolate Fe-S bond length and blue-shift the ligand-to-metal charge-transfer band (without loss of intensity). S K-edge X-ray absorption spectroscopy and density functional theory calculations show that, although the modified RS-O- fragment is incapable of forming a π bond with the FeIII center, the unmodified thiolate compensates for this loss of π bonding by increasing its covalent bond strength. The redox potential shifts only slightly (75 mV), and the magnetic properties are not affected (the S = 1/2 spin state is maintained). The coordinated sulfenate S-O bond is activated and fairly polarized (S +-O-). Addition of strong acids at low temperatures results in the reversible protonation of sulfenate-ligated 5. An X-ray structure demonstrates that Zn2+ binds to the sulfenate oxygen to afford [FeIII(ADIT)(ADIT-O-ZnCl3)] (6). The coordination of ZnCl3- to the RS-O- unit causes the covalent overlap with the unmodified thiolate to increase further. A possible catalytic role for the unmodified NHase thiolate, involving its ability to tune the electronics in response to protonation of the sulfenate (RS-O-) oxygen and/or substrate binding, is discussed.
