High resolution mass spectrometry characterization of the oxidation pattern of methionine and cysteine residues in rat liver mitochondria voltage-dependent anion selective channel 3 (VDAC3)

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• 作者：Rosaria Saletti^a ; ^{rsaletti@unict.it} ; Simona Reina^b ; ^c ; ^{simonareina@yahoo.it} ; Maria G.G. Pittalà ; ^a ; ^d ; ^{marinella.pitt@virgilio.it} ; Ramona Belfiore^c ; ^d ; ^{belfi88@hotmail.it} ; Vincenzo Cunsolo^a ; ^{vcunsolo@unict.it} ; Angela Messina^b ; ^c ; ^{mess@unict.it} ; Vito De Pinto^c ; ^d ; ^{vdpbiofa@unict.it} ; Salvatore Foti^a ; ^{sfoti@unict.it}
• 关键词：Voltage dependent anion selective channel isoform 3 (VDAC3) ; Amino acid redox state ; Cysteine ; Mitochondrial outer membrane ; Mitochondrial intermembrane space ; Orbitrap tribrid mass spectrometer
• 刊名：Biochimica et Biophysica Acta (BBA) - Biomembranes
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：1859
• 期：3
• 页码：301-311
• 全文大小：1061 K
• 卷排序：1859

文摘

Sulfur-containing amino acids in VDAC3 were investigated by enzymatic digestion and high resolution mass spectrometry. It was ascertained that methionine and cysteine residues in VDAC3 are in more redox states. The structural features elucidated may contribute to a better understanding of the VDAC3 functional properties.