By John Lloyd, John Mitchinson, James Harkin
A blinding 3rd installment of impressive new evidence from the New York Times best-selling authors of 1,227 fairly fascinating evidence to Blow Your Socks Off and 1,339 rather attention-grabbing proof to Make Your Jaw Drop.
1,411 really attention-grabbing proof to Knock You Sideways is a gold mine of wide-ranging, eye-opening, brain-bursting nuggets of minutiae that's very unlikely to place down, one other "treasure trove of factoids" (National Public Radio, Weekend Edition).
Did you recognize?
• Orchids can get jet lag
• Lizards can't stroll and breathe on the related time
• Frank Sinatra took a bath 12 occasions a day
• Ladybug orgasms final for 30 minutes
• There are 177,147 how one can tie a tie
• site visitors lighting existed earlier than cars
• The soil on your backyard is two million years previous
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Additional info for 1,411 Quite Interesting Facts to Knock You Sideways
The latter is often called "electron activation" and the resulting potential has been liberally placed at - 400 mV (157) or at - 700 mV (183). ATP-induced conformational changes at the substrate-reducing site have been proposed to bring metal coordination centers into an appropriate position for substrate binding (148), or to change the ligand configuration of a transition metal, such as to create the reductive species (173). The action of ATP as proton source at a non-aqueous dinitrogen reducing site has been suggested (1 76), as well as the intervention of solvated electrons (177).
ATP-induced shift of the redox potential of the Fe protein. (A) The Fe protein (180 ~M) in a solution of seven mediators (Em7 range - 444 to - 137 mV) was titrated oxidatively with ferricyanide. 87 resonance was plotted. The titration was reversible to 80%. 01. (B) The same system titrated in the presence of 2 mM ATP and 2 mM MgCI2. 93 resonance was plotted, The titration was reversible to 90%. 04. 5. The solid lines are theoretical one-electron transitions calculated on the basis of the indicated midpoint potentials.
4. The multiple-site hypothesis of nitrogenase-catalyzed reductions. Carbon monoxide divides the enzyme into an electron activating part and a substrate reducing part. Carbon monoxide also clearly separates the H 2 evolution site from the other substrate reducing sites. The mutual inhibition among the substrates, with the type of inhibition indicated in the lower half (c, competitive inhibition; nc, noncompetitive inhibition), separates the N 2 site from the C2H 2 site and these in turn from the HCN, N3-, and CH3NC site.
1,411 Quite Interesting Facts to Knock You Sideways by John Lloyd, John Mitchinson, James Harkin