How Does Single Oxygen Atom Addition Affect the Properties of an Fe–Nitrile Hydratase Analogue? The Compensatory Role of the Unmodified Thiolate
| Autor: | Priscilla Lugo-Mas, Werner Kaminsky, Keith O. Hodgson, Julie A. Kovacs, Britt Hedman, Edward I. Solomon, Jason B. Benedict, Abhishek Dey, Liang Xu, Steven D. Davin |
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| Jazyk: | angličtina |
| Rok vydání: | 2006 |
| Předmět: |
biology
Singlet Oxygen Chemistry Singlet oxygen Stereochemistry Iron Inorganic chemistry Active site Protonation General Chemistry Biochemistry Catalysis Article chemistry.chemical_compound Colloid and Surface Chemistry Oxidation state Nitrile hydratase Covalent bond biology.protein Sulfenic acid Sulfhydryl Compounds Hydro-Lyases Cysteine |
| Popis: | Nitrile hydratase (NHase) is one of a growing number of enzymes shown to contain post-translationally 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 pi bond with the Fe(III) center, the unmodified thiolate compensates for this loss of pi 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 Zn(2+) binds to the sulfenate oxygen to afford [Fe(III)(ADIT)(ADIT-O-ZnCl(3))] (6). The coordination of ZnCl(3)(-) 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. |
| Databáze: | OpenAIRE |
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