Nitric oxide (NO) binds to metalloproteins, and particularly to hemoproteins in both ferrous and ferric states, with association and dissociation rate constants which cover many orders of magnitude. These chemical properties often provide clear explanations of enzymatic specificity. A basic and straightforward description of the versatility of NO chemistry and of the biological relevance of NO effects, as understood by biochemists as opposed to physiologists, is presented. NO effects on hemoglobin and soluble guanylate cyclase, two proteins directly involved in arterio-venous oxygen transport at quite different biological levels, are compared. NO and other N-oxides also play primary roles in several mitochondrial functions. Specific interactions with cytochrome c oxidase and cytochrome c are reviewed, and the effects of NO and other N-oxides on other iron-cluster-containing components of mitochondrial respiration are discussed.