Posted on 04/20/2004 7:57:14 PM PDT by PatrickHenry
This article may point to yet another weakness in the "irreducable complexity" argument of Intelligent Design advocates.
So are liberals.
There's nothing in the bible that says Adam and Eve was God's first and only attempt at creation.
Their lineage diverged long ago from a common ancestor...
The ability to use oxygen for respiration allowed the diversity of life to expand vastly.
Early hemoglobins most likely evolved to bind and detoxify these gases...
... Hood said, and hemoglobins evolved into oxygen carriers rather than detoxifiers...
... “LUCA is believed to have been a metabolically ‘flexible’ single-celled organism with the ability to utilize oxygen for energy before free oxygen even existed in the air,...
Amazing amount of certainty in these statements. You have to admire someone with that much faith. I guess we are all just to smile and nod when such doctrines are stated.
I wonder if Evol-Doers have monasteries where the faithful can live simple lives and ponder the wonders of their faith to achieve this level of metaphysical certitude.
Instead of saying 'Thus saith the Lord', they just use an 'everybody knows Evolution happened, it is an insult to our intelligence to ask for details to back up our assumptions!' Pay no attention to the man behind the curtain.
So are liberals.
HAHAHAHA!
It's a real leap of faith to believe that in such a large universe (of which only 2.5% is ever going to be accessible, sensible or visible to us) that life wasn't developed/designed elsewhere, probably several times. No doubt it will even outlast the heat-death of the present physical universe in which we find ourselves ~ it's that well designed!
I agree. It's very annoying when people use imprecise language. It's like saying 'everybody knows' the earth is round, but did they run it by these people??
Thanks for bringing this to our attention, and don't let the creationists get you down.
Elizabeth Hood, who directs the areas of signal transduction and cellular regulation for NSF’s Division of Molecular and Cellular Biosciences, said, “As early life forms were established on earth, the atmosphere contained numerous toxic molecules, including nitric oxide and hydrogen sulfide. Early hemoglobins most likely evolved to bind and detoxify these gases. When oxygen became a component of the atmosphere, it was also toxic, and these early organisms used hemoglobin to bind and ultimately detoxify the oxygen.”
Hemoglobin is the Protein Data Bank's Molecule of the Month. (How could we have missed that???)
It mentions something interesting that I didn't know:
Use and Abuse of HemoglobinAside from oxygen transport, hemoglobin can bind and transport other molecules like nitric oxide and carbon monoxide. Nitric oxide affects the walls of blood vessels, causing them to relax. This in turn reduces the blood pressure. Recent studies have shown that nitric oxide can bind to specific cysteine residues in hemoglobin and also to the irons in the heme groups, as shown in PDB entry 1buw. Thus, hemoglobin contributes to the regulation of blood pressure by distributing nitric oxide through blood. Carbon monoxide, on the other hand, is a toxic gas. It readily replaces oxygen at the heme groups, as seen in PDB entry 2hco and many others, forming stable complexes that are difficult to remove. This abuse of the heme groups blocks normal oxygen binding and transport, suffocating the surrounding cells.
Is this what you're referring to?
Hemoglobin CousinsLooking through the PDB, you will find many different hemoglobin molecules. You can find Max Perutz's groundbreaking structure of horse hemoglobin in entry 2dhb, shown in the picture here. There are structures of human hemoglobins, both adult and fetal. You can also find unusual hemoglobins like leghemoglobin, which is found in legumes. It is thought to protect the oxygen-sensitive bacteria that fix nitrogen in leguminous plant roots. In the past few years some hemoglobin cousins called the "truncated hemoglobins" have been identified, such as the hemoglobin in PDB entry 1idr, which have several portions of the classic structure edited out. The only feature that is absolutely conserved in this subfamily of proteins is the histidine amino acid that binds to the heme iron.
And, if the article had used the words "might" or "maybe" you'd be lambasting the researchers for making up "just-so" stories.
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