End of Round II ready for Round III
Hello everyone!!
The semester is just about wrapping up, so things are getting a little hectic in the classroom. As for research, I was able to fulfill all my goals that were set for this semester. I successfully calculated the formation constant of sulfmyoglobin in oxygen. According to my mentor, this had not yet been researched by any known colleague of his. I’m a little excited about this, since it means I might be able to publish something next semester (after much honing and polishing of course!). We’ll see, I will certainly let everyone know if it will work out. Next semester I will begin repeating the kinetic experiments, varying the reagents and their respective concentrations.
I would love to explain in full what my experiments consisted of so that there may be a joint understanding of my accomplishments. I was tempted to post my final report to protoporphyrin9 but I don’t think it would be wise to make it open access just yet. But, in a nutshell my experiments consisted on kinetic studies of the synthesis reaction of sulfmyoglobin. A condensed version of this reaction is as follows:
MbFeII (a) O2 MbFeIIO2 (b) H2S MbFeIIO-O-• + HS• k1= 0.643654004s-1M-1 SMbA + SMbC
Pretty simple eh? This equation displays the reaction with a single initial oxidation state of the iron atom of myoglobin ( +2 ). This oxidation state can vary in accordance to the species that are present in the solution. In my case, I conducted the kinetic study in the presence of two oxidation states of myoglobin ( + 2 and +3 ). Next semester I will want to repeat the experiments with only one oxidation state present. This is much easier to explain with UV/VIS spectra! The reason I am emphasizing this is because there are certain absorption bands that are present at (+2) that are completely different from the absorption bands at (+3).
Now, supposedly there should be little or no difference in my results if I use a single or double oxidation state of myoglobin. Why? Well the formation constant of Mb is actually the slope of a graph of rate constants vs hydrogen sulfide concentration. What does this mean? This means that if my absorptions vary in a uniform way then the slope of the graph would remain generally unaffected. This does not discredit my work this semester because I was able to achieve linear graphs and my formation constant is representative of a slow synthesis reaction (which it is!) . A formation constant less than 0.7M-1s-1 ; is considered pretty slow.
Questions and questions that I know can get to be a little confusing, but it does merit the chance to be further analyzed with more time…right? I plan to get right on it in January with no time to waste. I am sufficiently confident to take this experiment and keep running with it, analyzing the variables and different possibilities. But as for the work this semester I would consider it a great contribution to the field of biochemical science. I was able to quantitatively determine the rate and formation constant of a synthesis reaction involving a hemeprotein.
Well that’s all I have to provide for the moment. Next semester proves to be an exciting one.
May everyone have a Happy Thanksgiving, Merry Christmas & Happy New Year.
Catch ya’ll later
Chris
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