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Yes, FAD is a dione... let me think now. c.f. Quinone
-- Rolodexx ( talk) 23:03, 16 December 2011 (UTC)
Someone needs to cite a source for the ATP equivalents because I'm 99% sure it's wrong. I'm looking at a Figure 17-7 for those who have Voet-Voet's Biochemistry (2e). If I'm reading it right, the electrons are passed from one FADH2 in Complex II to CoQ. 1.0 ATP is generated from the transfer to Cytochrome C via Complex III, and 1.0 more following the transfer to water, via Complex IV for a total of 2.0 ATP equivalents. -- Michael ( talk) 19:28, 9 March 2009 (UTC)
Perhaps someone could add a section about the 'ability' of this molecule to accept one electron so that it becomes a half-reduced (relatively stable) radical. This way it connects metal electron transfer with organic electron transfer. —Preceding unsigned comment added by 80.126.164.111 ( talk) 22:48, 27 October 2009 (UTC)
The result of the move request was: page moved. Rifleman 82 ( talk) 14:29, 22 August 2012 (UTC)
Moved per lack of opposition and in conformance with Wikipedia:Article_titles (abbreviations). -- Rifleman 82 ( talk) 14:29, 22 August 2012 (UTC)
FAD → Flavin adenine dinucleotide –
We are working on expanding the coverage of this page as part of a class from January to February 2015. This is a rough outline of our planned additions:
Thanks! Gk2015 ( talk) 00:09, 19 January 2015 (UTC)
As of 2/25/15, we just uploaded our additions to the page. Gk2015 ( talk) 01:43, 26 February 2015 (UTC)
Picture size: pictures are too big to be helpful and obscure much of the page — Preceding unsigned comment added by SireWonton ( talk • contribs) 16:53, 27 October 2015 (UTC)
The comment(s) below were originally left at Talk:Flavin adenine dinucleotide/Comments, and are posted here for posterity. Following several discussions in past years, these subpages are now deprecated. The comments may be irrelevant or outdated; if so, please feel free to remove this section.
Rated "high" as high school/SAT biology content - tameeria 19:53, 22 February 2007 (UTC) |
Substituted at 05:10, 13 May 2016 (UTC)
This section seems to imply that CPR and CP-450 are the same protein, and contain two flavins and a heme. It is my understanding that CP-450 contains only heme, and CPR (Cyt P450 Reductase) contains FMN and FAD which are involved in transferring electrons from NAD(P)H to CP-450. Could someone verify this and update the section? Eaberry ( talk) 17:57, 21 January 2017 (UTC)
In the section Properties, it states
> FAD is an aromatic ring system, whereas FADH2 is not.
I've been able to trace this to a book quote, Bioprocess Engineering, which states
> FAD is an aromatic ring (flavin group) system, whereas FADH2 is not.
The image
clearly shows an "aromatic" benzene group on the left hand side of both molecules, and the right hand side of FADH2 is Uracil, which although the article on uracil doesn't suggest it is aromatic, there are citations that support uracil's aromaticity, e.g. [1] [2]
I haven't been able to uncover the truth of the assertion one way or the other elsewhere in primary literature, and think this should be a "citation needed" or some other qualifier until this can be verified in a conclusive matter. I have blogged about this question elsewhere, e.g. https://www.quora.com/Is-FADH2-aromatic/answer/Matt-Harbowy
MatthewEHarbowy ( talk) 22:08, 25 June 2020 (UTC)
References