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首页> 外文期刊>Biology Bulletin >Purification and Properties of Membrane-Bound Methane Hydroxylase from Methylococcus capsulatus (Strain M)
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Purification and Properties of Membrane-Bound Methane Hydroxylase from Methylococcus capsulatus (Strain M)

机译：荚膜甲基球菌（M菌株）膜结合甲烷羟化酶的纯化及性质

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摘要

Membrane fraction of Methylococcus capsulatus (strain M) were treated with [~(14)C]acetylene, an affinity label binding to the active center of membrane-bound methane monooxygenase (MMO). High-purity paniculate form of methane hydroxylase (pMH) was obtained by ion exchange and hydrophobic chromatogra-phy. According to SDS-PAGE data, the enzyme contained three polypeptides with molecular weights of 47 (a), 27 (β), and 25 (Υ) kDa in the ratio 1:1:1. The radiolabel was contained in the P-subunit of pMH. The protein contained 1 or 2 atoms of nonheme iron and 2-4 atoms of copper per a minimum molecular weight of 99 kDa. This protein did not oxidize methane or propylene in the presence of NADH but was able to oxidize low quantities of methane in the presence of duroquinol. It was established that methanol dehydrogenase (MD) and NADH oxidoreductase (NADH-OR) are peripheral membrane proteins. Possible causes of low activity of high-purity methane hydroxylase are discussed.
机译：用[〜（14）C]乙炔处理荚膜甲基球菌（M株）的膜部分，乙炔是与膜结合的甲烷单加氧酶（MMO）活性中心结合的亲和标记。通过离子交换和疏水色谱法获得高纯度的甲烷羟化酶（pMH）颗粒形式。根据SDS-PAGE数据，该酶包含三种多肽，其分子量分别为1：1：1和47（a），27（β）和25（Υ）kDa。放射性标记包含在pMH的P亚基中。蛋白质的最小分子量为99 kDa，包含1或2个非血红素铁原子和2-4个铜原子。该蛋白质在NADH存在下不会氧化甲烷或丙烯，但在度洛喹诺醇存在下却能够氧化少量甲烷。已确定甲醇脱氢酶（MD）和NADH氧化还原酶（NADH-OR）是外周膜蛋白。讨论了高纯度甲烷羟化酶活性低的可能原因。

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