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細菌的代謝與遺傳
細菌的代謝與遺傳
江倪全
2012-09-25
101 學年 第?一學期
1
代謝、能量及生物合成
2
代謝與分類
O2
O2
絕對厭氧菌 (Obligate anaerobes)
莢膜梭菌(Clostridium perfringens)
絕對需氧菌 (Obligate aerobes)
結核桿菌(Mycobacterium tuberculosis)
兼性厭氧菌 (Facultative anaerobes)
can be further metabolised and excreted in the urine. Proteins
such as transferrin and albumin in extracellular fluids sequester
transition metal ions thereby preventing them from catalysing
generation of hydroxyl radicals [19].
3.1. Mitochondrial anti-oxidant defence mechanisms
As the major site of ROS generation, it is not surprising
that the mitochondrion has its own anti-oxidant defence
mechanisms. Superoxide dismutase again plays a major role in
anti-oxidant defence, but although SOD1 is found in the
intermembrane space [15,20,21] where it can remove superox-
ide generated at the outer face of the inner mitochondrial
membrane [22], it is SOD2, present in the mitochondrial matrix,
that is the major mitochondrial SOD enzyme [23,24]. Since
superoxide does not readily cross cell membranes, SOD2 has a
vital role in anti-oxidant defence in mitochondria, evident in that
SOD2 knock-out mice develop mitochondrial deficiencies
associated with ROS toxicity and die in early postnatal life
[25,26]. Catalase is not present within mitochondria, so the
hydrogen peroxide produced by SOD2 is degraded by
glutathione peroxidases [27,28] or peroxiredoxin 3 (Prx3)
[29,30] within the mitochondrial matrix. Prx3 homodimers
catalyse removal of hydrogen peroxide in a mechanism
reminiscent of glutathione peroxidase; hydrogen peroxide
oxidises the thiol group on an N-terminal conserved cysteine
residue in one Prx3 subunit, which in turn reacts with a second
conserved thiol group at the C-terminal of the other Prx subunit
(Fig. 3B.III). The oxidised Prx3 is then recycled by reaction with
thioredoxin (Trx), which is itself recycled to its reduced form by
thioredoxin reductase. Whilst the peroxidase activity of Prx3 is
low compared to that of catalase and the glutathione peroxidases
[2
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