Wada K
J Biochem. 1979 Dec;86(6):1747-52. doi: 10.1093/oxfordjournals.jbchem.a132695.
The effects of metal ions on the thermal denaturation and Mg2+ binding of native spinach ferredoxin and its acetylated derivative were investigated. The denaturation of ferredoxin in a metal-free solution at 40 degrees C was quickly prevented by the addition of Mg2+ or Na+ at appropriate concentrations. The metal concentrations required for 50% protection from thermal denaturation were 1.54 x 10(-4) M Mg2+ or 8.0 x 10(-3) M Na+ for native ferredoxin and 1.05 x 10(-3) M Mg2+ or 6.0 x 10(-2) M Na+ for acetylated ferredoxin. It was also found that native ferredoxin in the presence of over 20 mM Mg2+ was almost completely protected from thermal denaturation at 40 degrees C. The D-form which has been observed in acetylated ferredoxin by Masaki et al. (1977) (J. Biochem. 81, 1-9) was confirmed to be present in native ferredoxin at high temperature (49 degrees C) and is suggested to be an important form in the denaturation processes of the ferredoxin molecule.
研究了金属离子对天然菠菜铁氧化还原蛋白及其乙酰化衍生物的热变性和Mg2+结合的影响。在无金属溶液中，40℃下铁氧化还原蛋白的变性可通过加入适当浓度的Mg2+或Na+迅速阻止。对于天然铁氧化还原蛋白，防止50%热变性所需的金属浓度为1.54×10(-4) M Mg2+或8.0×10(-3) M Na+；对于乙酰化铁氧化还原蛋白，则为1.05×10(-3) M Mg2+或6.0×10(-2) M Na+。还发现，在超过20 mM Mg2+存在下，天然铁氧化还原蛋白在40℃几乎完全受到热变性保护。Masaki等人（1977年）（《生物化学杂志》81卷，1-9页）在乙酰化铁氧化还原蛋白中观察到的D型，在天然铁氧化还原蛋白高温（49℃）时也被证实存在，并且被认为是铁氧化还原蛋白分子变性过程中的一种重要形式。
