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From: "A.Appleyard" <A.APPLEYARD@fs*.mt*.um*.ac*.uk*>
To: techdiver@terra.net
Date: Fri, 10 Nov 1995 08:25:52 GMT
Subject: Re: O2 toxicity (biochemistry)
  A.APPLEYARD@fs*.mt*.um*.ac*.uk* wrote:-
> If so, perhaps sometimes another O2 molecule hits the
> O2-Fe-Cu-cytochrome-etc complex hard enough to knock the `sitting tenant' O2
> molecule out and replace it before it has picked up 4 electrons [thus
> producing a superoxide ion O2-]. ...

  Anthony Montgomery <amontgom@ha*.ed*> replied:-
> The O2 binds in the Fe-Cu complex just like it does between the Fe-His E7 in
> Mb and Hb. As you know this is a very strong bond. It is possible that an O2
> or O-2 molecule could be knock out, but this won't yield a Superoxide anion
> ...

  The sitting O2 has time to pick up one electron and become O2-, then it is
knocked out of the complex. Result is one loose O2- (superoxide) ion.

> in another chemistry book. It talks about the Superoxide dimutase which
> protects us from the Superoxide Anion ...

  I think this should be `dismutase'. It turns 2 O2- + 2 H+ into O2 + HOOH.
There is also a peroxide dismutase that turns 2 HOOH into O2 + 2 HOH.

> the books say that the catalyst must not release partially reduced
> intermediates. So if the Fe-Cu complex can release the Superoxide anion,
> then how is that done exactly?

  The speeds of thermal motions of molecules are distributed on a frequency
pattern, and occasionally there is one fast enough to knock the O2 out of the
complex before it has received all 4 electrons to turn it into 2 HOH. Normally
likely the O2 (or whatever intermediate stage it has reached) at once goes
back into the complex again, but if the body fluid ppO2 is high and there is a
lot of free O2 about, a different O2 molecule may get into the complex first
and leave a free O2- or HOOH or HO to cause what damage it can unless the
dismutase enzymes find it first.

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