PubMed · 1781019
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R A Bradshaw. 1991. All good things .... https://doi.org/10.1016/0968-0004(91)90174-t
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The Human Genome Project, DNA microarrays, proteome chips and metabolic profiles, among others, are generating unprecedented amounts of valuable information about the genetic and metabolic responses of organisms to stimuli. This wealth of information poses a great scientific challenge, namely the development of novel, effective methods for functional analysis and interpretation. It is proposed here that biomathematical systems models must accompany data generation and management. A particularly effective framework for this purpose is canonical modeling based on Biochemical Systems Theory. The key concept of this theory is the formulation of biological phenomena as systems of differential equations, in which all processes are represented as products of power-law functions.
Biomineralization of the ferritin iron core involves a complex series of events in which H(2)O(2) is produced during iron oxidation by O(2) at a dinuclear centre, the 'ferroxidase site', located on the H-subunit of mammalian proteins. Rapid-freeze quench Mössbauer spectroscopy was used to probe the early events of iron oxidation and mineralization in recombinant human ferritin containing 24 H-subunits. The spectra reveal that a mu-1,2-peroxodiFe(III) intermediate (species P) with Mössbauer parameters delta (isomer shift)=0.58 mm/s and DeltaE(Q) (quadrupole splitting)=1.07 mm/s at 4.2 K is formed within 50 ms of mixing Fe(II) with the apoprotein. This intermediate accounts for almost all of the iron in the sample at 160 ms. It subsequently decays within 10 s to form a mu-oxodiFe(III)-protein complex (species D), which partially vacates the ferroxidase sites of the protein to generate Fe(III) clusters (species C) at a reaction time of 10 min. The intermediate peroxodiFe(III) complex does not decay under O(2)-limiting conditions, an observation suggesting inhibition of decay by unreacted Fe(II), or a possible role for O(2) in ferritin biomineralization in addition to that of direct oxidation of iron(II).
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