Myoglobin-carbon monoxide reaction

Since enthalpy changes can be obtained directly from measurement of heat absorption at constant pressure, even small values of AH for chemical and biochemical reactions can be measured using a micro-calorimeter.1112 Using the technique of pulsed acoustic calorimetry, changes during biochemical processes can be followed on a timescale of fractions of a millisecond. An example is the laser-induced dissociation of a carbon monoxide-myoglobin complex.13... 

In the present section some applications of the previously outlined theoretical framework, recently reported in literature [24,25], will be illustrated. In particular we will focus our attention on two benchmark reactions of computational-theoretical chemistry, namely the carbon monoxide (CO) binding-unbinding reaction in myoglobin (Mb) and the unimolecular tautomeric proton transfer in aqueous malonaldehyde. 

Spencer and Schaumburg 2000). Although the primary reaction of carbon monoxide is with hemoglobin, it also interacts with myoglobin, cytochromes, and metalloenzymes (e.g., cytochrome c oxidase and cytochrome P450) (WHO 1999). The health importance of these secondary reactions is not well understood. 

The performance of the pneumatic system, mixing and transfer systems may be tested by using any reaction with a moderately short half time, say 10-20 ms, e.g. the reaction between 2,6-dichlorophenolindophenol, DCIP, and i-ascorbate. Here we illustrate using the reaction between myoglobin and carbon monoxide, but any reaction taking some 50 ms or less to complete may be substituted ... 

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