Hi Martin

This brought back memories of my PhD when I was synthesising metallorganic 
molecules (quite, quite different from the species that are described nowadays 
as “metal-organic frameworks”) which had M-M distances in the range 2.8 - 3.1 
Å). These species wouldn’t have survived a close encounter with a protein 
unless it had been dehydrated thoroughly and was under an argon atmosphere.  

Best wishes

Harry

> On 20 Dec 2024, at 12:09, Martin Malý <martin.maly...@email.cz> wrote:
> 
> Dear Harry,
> 
> You can check this structure of an FAD-dependent monooxygenase with bound FAD 
> and NADPH: https://www.rcsb.org/structure/1k0j
> However, authors of this review (https://doi.org/10.3390/ijms131215601) seem 
> not to be convinced about the NADPH position (if I remember that review 
> right). 
> 
> By the way, I would be interested in metal-metal interactions in biomolecules 
> (if I can a bit hijack this thread...) I do not mean interactions like 
> Mg-Cl-Mg, but clearly two metal atoms closer than ~3.6 A to each other.
> 
> Best wishes,
> Martin
> 
> 
> On 20/12/2024 11:07, Chandra Prakash Tiwari wrote:
>> Yes, multiple cofactors can exist in active sites. One example is Enolase. 
>> Also, metal-metal bonds are common in coordination spheres for catalysis. 
>> 
>> On Fri, Dec 20, 2024 at 4:34 PM David Briggs <david.bri...@crick.ac.uk> 
>> wrote:
>> Hi Harry,
>> 
>> The first thing that comes to mind is any sort of light harvesting complex - 
>> take a look at 1RWT. Would that fit the bill?
>> 
>> D
>> 
>> 
>> 
>> --
>> Dr David C. Briggs CSci MRSB (he/him)
>> Principal Laboratory Research Scientist
>> Signalling and Structural Biology Lab
>> The Francis Crick Institute
>> London, UK
>> Working hours: Mon-Fri 0900-1700
>> ==
>> about.me/david_briggs | OrcID | Google Scholar 
>> ==
>> "Would it not be better if one could really 'see' whether molecules...were 
>> just as experiments suggested?"
>> – Dorothy Hodgkin
>> From: CCP4 bulletin board <CCP4BB@JISCMAIL.AC.UK> on behalf of Harry Powell 
>> <0000193323b1e616-dmarc-requ...@jiscmail.ac.uk>
>> Sent: 20 December 2024 10:37
>> To: CCP4BB@JISCMAIL.AC.UK <CCP4BB@JISCMAIL.AC.UK>
>> Subject: [ccp4bb] enzyme or other protein with multiple cofactors
>>  
>> 
>> External Sender: Use caution.
>> 
>> 
>> Hi folks
>> 
>> I’m familiar with enzymes that have a single co-factor (for example haem in 
>> myoglobin [or in the individual chains in haemoglobins] or FAD in 
>> flavoproteins), but was wondering if there are examples of single-chain 
>> proteins that have multiple cofactors (or even multiple chain proteins that 
>> have multiple cofactors bound to a single chain)?
>> 
>> I’m not bothered (at the moment) about proteins that have cofactors bound to 
>> different chains.
>> 
>> I thought this would be a good place to ask…
>> 
>> Harry
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